Q9UQ35 (SRRM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/arginine repetitive matrix protein 2

Alternative name(s):
300 kDa nuclear matrix antigen
Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa
Short name=SR-related nuclear matrix protein of 300 kDa
Short name=Ser/Arg-related nuclear matrix protein of 300 kDa
Splicing coactivator subunit SRm300
Tax-responsive enhancer element-binding protein 803
Short name=TaxREB803

Gene names

Name:	SRRM2
Synonyms:	KIAA0324, SRL300, SRM300
ORF Names:	HSPC075

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2752 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome. May do so by stabilizing the catalytic center or the position of the RNA substrate By similarity. Binds to RNA. Ref.2
Subunit structure	Component of the active spliceosome. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1, SRRM1 and SRRM2. Identified in the spliceosome C complex. Ref.9 Ref.10
Subcellular location	Nucleus speckle.
Tissue specificity	Expressed in liver, placenta, and white blood cells. Ref.1
Miscellaneous	Can functionally substitute for CWC12 in yeast (Ref.19).
Sequence similarities	Belongs to the CWC21 family.
Sequence caution	The sequence AAF21439.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAF28898.1 differs from that shown. Reason: Frameshift at positions 167, 175 and 179. The sequence AAH70050.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence BAA20782.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splicing, via spliceosome Inferred by curator Ref.10. Source: UniProtKB
Cellular_component	Cajal body Inferred from direct assay PubMed 17577209. Source: UniProtKB catalytic step 2 spliceosome Inferred from direct assay Ref.10. Source: UniProtKB nuclear speck Inferred from direct assay PubMed 17577209. Source: UniProtKB
Molecular_function	C2H2 zinc finger domain binding Inferred from direct assay PubMed 17577209. Source: UniProtKB RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAK1	Q16611	1	EBI-1050142,EBI-519866
RNPS1	Q15287	1	EBI-1050142,EBI-395959
YWHAB	P31946	1	EBI-1050142,EBI-359815
YWHAG	P61981	1	EBI-1050142,EBI-359832

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UQ35-1)

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: Q9UQ35-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2023-2440: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9UQ35-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: Missing.
     394-407: PSEASPTRDRSPPK → SPQLFMFLKGILVF
     408-2752: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2752	2752	Serine/arginine repetitive matrix protein 2		PRO_0000248154
Regions
	Region	197 – 259	63	Sufficient for RNA-binding
	Coiled coil	60 – 92	33	Potential
	Compositional bias	177 – 2731	2555	Ser-rich
	Compositional bias	186 – 246	61	Lys-rich
	Compositional bias	350 – 447	98	Pro-rich
	Compositional bias	462 – 816	355	Arg-rich
	Compositional bias	1666 – 2089	424	Arg-rich
	Compositional bias	2182 – 2378	197	Ala-rich
	Compositional bias	2673 – 2750	78	Arg-rich
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.7 Ref.25
	Modified residue	24	1	Phosphoserine
	Modified residue	145	1	Phosphotyrosine Ref.20
	Modified residue	169	1	N6-acetyllysine Ref.21
	Modified residue	220	1	Phosphoserine Ref.22
	Modified residue	222	1	Phosphoserine Ref.22
	Modified residue	286	1	Phosphothreonine Ref.22
	Modified residue	295	1	Phosphoserine Ref.17 Ref.22
	Modified residue	297	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	300	1	Phosphoserine Ref.22
	Modified residue	322	1	Phosphoserine Ref.17 Ref.20
	Modified residue	323	1	Phosphoserine Ref.17 Ref.20
	Modified residue	333	1	Phosphoserine Ref.24
	Modified residue	351	1	Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	353	1	Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	357	1	Phosphoserine Ref.20
	Modified residue	358	1	Phosphoserine Ref.20
	Modified residue	359	1	Phosphothreonine Ref.20
	Modified residue	367	1	Phosphothreonine Ref.13 Ref.20 Ref.22
	Modified residue	377	1	Phosphoserine Ref.13 Ref.15 Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	387	1	Phosphoserine Ref.17
	Modified residue	398	1	Phosphoserine Ref.17 Ref.24
	Modified residue	404	1	Phosphoserine Ref.24
	Modified residue	408	1	Phosphoserine Ref.24
	Modified residue	424	1	Phosphoserine Ref.22 Ref.24
	Modified residue	435	1	Phosphoserine Ref.17
	Modified residue	436	1	Phosphoserine By similarity
	Modified residue	437	1	Phosphoserine By similarity
	Modified residue	440	1	Phosphoserine Ref.12 Ref.17 Ref.22 Ref.24
	Modified residue	454	1	Phosphoserine Ref.22
	Modified residue	484	1	Phosphoserine Ref.22
	Modified residue	486	1	Phosphoserine Ref.22
	Modified residue	534	1	Phosphoserine By similarity
	Modified residue	536	1	Phosphoserine By similarity
	Modified residue	778	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	780	1	Phosphoserine Ref.17
	Modified residue	783	1	Phosphoserine Ref.17 Ref.24
	Modified residue	846	1	Phosphoserine Ref.20
	Modified residue	857	1	Phosphoserine Ref.17 Ref.20
	Modified residue	864	1	Phosphoserine Ref.17
	Modified residue	866	1	Phosphothreonine Ref.17 Ref.20 Ref.22
	Modified residue	871	1	Phosphoserine Ref.13 Ref.22
	Modified residue	875	1	Phosphoserine Ref.22
	Modified residue	876	1	Phosphoserine Ref.13 Ref.20 Ref.22 Ref.24
	Modified residue	908	1	Phosphoserine Ref.24
	Modified residue	924	1	Phosphoserine
	Modified residue	950	1	Phosphoserine Ref.17 Ref.22
	Modified residue	952	1	Phosphoserine Ref.17 Ref.20
	Modified residue	954	1	Phosphoserine Ref.13 Ref.17 Ref.20
	Modified residue	957	1	Phosphoserine Ref.17
	Modified residue	968	1	Phosphoserine Ref.17
	Modified residue	970	1	Phosphoserine Ref.17
	Modified residue	972	1	Phosphoserine Ref.17
	Modified residue	973	1	Phosphoserine Ref.22 Ref.24
	Modified residue	974	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	977	1	Phosphothreonine Ref.24
	Modified residue	983	1	Phosphothreonine Ref.17 Ref.22
	Modified residue	992	1	Phosphoserine Ref.24
	Modified residue	994	1	Phosphoserine Ref.17 Ref.22
	Modified residue	1003	1	Phosphothreonine Ref.12 Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	1014	1	Phosphoserine Ref.17 Ref.22
	Modified residue	1028	1	Phosphoserine Ref.17 Ref.22
	Modified residue	1032	1	Phosphoserine Ref.17
	Modified residue	1043	1	Phosphothreonine Ref.24
	Modified residue	1064	1	Phosphoserine Ref.17
	Modified residue	1069	1	Phosphoserine Ref.17 Ref.24
	Modified residue	1072	1	Phosphoserine Ref.13 Ref.17
	Modified residue	1073	1	Phosphoserine Ref.13 Ref.17
	Modified residue	1083	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1099	1	Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	1101	1	Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	1102	1	Phosphoserine Ref.13 Ref.17 Ref.20
	Modified residue	1103	1	Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	1106	1	Phosphothreonine Ref.20
	Modified residue	1112	1	Phosphoserine Ref.17
	Modified residue	1122	1	Phosphoserine Ref.22
	Modified residue	1124	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1129	1	Phosphoserine Ref.24
	Modified residue	1132	1	Phosphoserine Ref.12 Ref.22 Ref.24
	Modified residue	1152	1	Phosphoserine Ref.22
	Modified residue	1179	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	1188	1	Phosphoserine Ref.12 Ref.17 Ref.22 Ref.24
	Modified residue	1208	1	Phosphothreonine Ref.17
	Modified residue	1214	1	Phosphoserine Ref.20
	Modified residue	1219	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1257	1	Phosphoserine By similarity
	Modified residue	1311	1	Phosphoserine By similarity
	Modified residue	1318	1	Phosphoserine Ref.17 Ref.20
	Modified residue	1320	1	Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	1326	1	Phosphoserine Ref.17 Ref.20 Ref.22
	Modified residue	1329	1	Phosphoserine Ref.12 Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	1336	1	Phosphoserine Ref.22
	Modified residue	1348	1	Phosphoserine By similarity
	Modified residue	1368	1	Phosphoserine Ref.22
	Modified residue	1382	1	Phosphoserine Ref.20 Ref.24
	Modified residue	1383	1	Phosphoserine By similarity
	Modified residue	1387	1	Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	1401	1	Phosphoserine Ref.17 Ref.20
	Modified residue	1403	1	Phosphoserine Ref.20
	Modified residue	1404	1	Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	1413	1	Phosphothreonine Ref.17 Ref.22 Ref.24
	Modified residue	1415	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	1421	1	Phosphoserine Ref.22
	Modified residue	1423	1	Phosphoserine By similarity
	Modified residue	1424	1	Phosphoserine Ref.24
	Modified residue	1434	1	Phosphothreonine Ref.22
	Modified residue	1444	1	Phosphoserine Ref.17 Ref.24
	Modified residue	1451	1	Phosphoserine Ref.17
	Modified residue	1453	1	Phosphothreonine Ref.17
	Modified residue	1458	1	Phosphoserine Ref.24
	Modified residue	1460	1	Phosphoserine Ref.22
	Modified residue	1462	1	Phosphoserine Ref.22
	Modified residue	1463	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1472	1	Phosphothreonine Ref.17
	Modified residue	1482	1	Phosphoserine Ref.22
	Modified residue	1483	1	Phosphoserine Ref.22
	Modified residue	1492	1	Phosphothreonine Ref.12 Ref.22
	Modified residue	1497	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1499	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1501	1	Phosphoserine Ref.22
	Modified residue	1502	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1511	1	Phosphothreonine Ref.17
	Modified residue	1517	1	Phosphoserine Ref.24
	Modified residue	1519	1	Phosphoserine Ref.24
	Modified residue	1521	1	Phosphoserine Ref.24
	Modified residue	1522	1	Phosphoserine Ref.17 Ref.24
	Modified residue	1531	1	Phosphothreonine Ref.14 Ref.17
	Modified residue	1537	1	Phosphoserine Ref.17
	Modified residue	1539	1	Phosphoserine Ref.17
	Modified residue	1541	1	Phosphoserine Ref.17
	Modified residue	1542	1	Phosphoserine Ref.17 Ref.24
	Modified residue	1552	1	Phosphoserine Ref.17 Ref.24
	Modified residue	1577	1	Phosphoserine Ref.24
	Modified residue	1579	1	Phosphoserine Ref.24
	Modified residue	1581	1	Phosphoserine Ref.24
	Modified residue	1582	1	Phosphoserine Ref.24
	Modified residue	1598	1	Phosphoserine Ref.24
	Modified residue	1600	1	Phosphoserine Ref.24
	Modified residue	1601	1	Phosphoserine Ref.24
	Modified residue	1616	1	Phosphoserine By similarity
	Modified residue	1620	1	Phosphoserine By similarity
	Modified residue	1621	1	Phosphoserine Ref.22
	Modified residue	1648	1	Phosphoserine Ref.24
	Modified residue	1658	1	Phosphoserine Ref.24
	Modified residue	1691	1	Phosphoserine Ref.17
	Modified residue	1693	1	Phosphoserine Ref.17
	Modified residue	1694	1	Phosphoserine Ref.17 Ref.24
	Modified residue	1698	1	Phosphothreonine Ref.17
	Modified residue	1727	1	Phosphoserine Ref.24
	Modified residue	1729	1	Phosphoserine Ref.24
	Modified residue	1731	1	Phosphoserine Ref.24
	Modified residue	1732	1	Phosphoserine Ref.24
	Modified residue	1762	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1764	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1818	1	Phosphoserine Ref.24
	Modified residue	1822	1	Phosphoserine Ref.24
	Modified residue	1854	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1857	1	Phosphoserine Ref.22
	Modified residue	1876	1	Phosphoserine Ref.17
	Modified residue	1878	1	Phosphoserine Ref.17 Ref.24
	Modified residue	1880	1	Phosphothreonine Ref.17
	Modified residue	1884	1	Phosphoserine Ref.24
	Modified residue	1890	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1892	1	Phosphothreonine Ref.22
	Modified residue	1893	1	Phosphoserine Ref.22
	Modified residue	1916	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1919	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1923	1	Phosphoserine Ref.17
	Modified residue	1925	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	1927	1	Phosphothreonine Ref.17 Ref.22 Ref.24
	Modified residue	1931	1	Phosphothreonine Ref.24
	Modified residue	1946	1	Phosphoserine Ref.17
	Modified residue	1948	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	1950	1	Phosphothreonine Ref.17 Ref.22 Ref.24
	Modified residue	1954	1	Phosphothreonine Ref.24
	Modified residue	1958	1	Phosphoserine Ref.17
	Modified residue	1960	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	1962	1	Phosphothreonine Ref.17 Ref.22 Ref.24
	Modified residue	1966	1	Phosphothreonine Ref.24
	Modified residue	1970	1	Phosphoserine Ref.17 Ref.24
	Modified residue	1972	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1975	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1978	1	Phosphothreonine Ref.24
	Modified residue	1984	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1987	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1996	1	Phosphoserine Ref.22 Ref.24
	Modified residue	1999	1	Phosphoserine Ref.22 Ref.24
	Modified residue	2008	1	Phosphoserine Ref.22 Ref.24
	Modified residue	2011	1	Phosphoserine Ref.22 Ref.24
	Modified residue	2020	1	Phosphoserine Ref.24
	Modified residue	2022	1	Phosphothreonine Ref.24
	Modified residue	2030	1	Phosphoserine By similarity
	Modified residue	2032	1	Phosphoserine Ref.24
	Modified residue	2034	1	Phosphothreonine Ref.24
	Modified residue	2044	1	Phosphoserine Ref.22 Ref.24
	Modified residue	2046	1	Phosphoserine Ref.22 Ref.24
	Modified residue	2067	1	Phosphoserine Ref.24
	Modified residue	2069	1	Phosphothreonine Ref.22 Ref.24
	Modified residue	2071	1	Phosphoserine Ref.22 Ref.24
	Modified residue	2090	1	Phosphoserine Ref.24
	Modified residue	2092	1	Phosphothreonine Ref.24
	Modified residue	2100	1	Phosphoserine Ref.17 Ref.20
	Modified residue	2102	1	Phosphoserine Ref.17 Ref.20 Ref.22
	Modified residue	2104	1	Phosphothreonine Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	2118	1	Phosphoserine Ref.17
	Modified residue	2121	1	Phosphoserine Ref.17
	Modified residue	2123	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	2132	1	Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	2144	1	Phosphothreonine Ref.17
	Modified residue	2272	1	Phosphoserine Ref.13 Ref.16 Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	2289	1	Phosphothreonine Ref.17 Ref.20 Ref.22
	Modified residue	2291	1	Phosphothreonine Ref.13
	Modified residue	2302	1	Phosphothreonine Ref.17 Ref.22
	Modified residue	2316	1	Phosphothreonine Ref.13 Ref.17 Ref.20
	Modified residue	2329	1	Phosphothreonine Ref.17 Ref.22
	Modified residue	2335	1	Phosphoserine Ref.22
	Modified residue	2343	1	Phosphoserine Ref.22
	Modified residue	2381	1	Phosphothreonine Ref.20
	Modified residue	2382	1	Phosphoserine Ref.13 Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	2394	1	Phosphoserine Ref.22
	Modified residue	2398	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	2407	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	2409	1	Phosphothreonine Ref.17 Ref.22
	Modified residue	2412	1	Phosphoserine Ref.17 Ref.24
	Modified residue	2415	1	Phosphoserine Ref.24
	Modified residue	2426	1	Phosphoserine Ref.24
	Modified residue	2429	1	Phosphoserine Ref.24
	Modified residue	2449	1	Phosphoserine Ref.15 Ref.17 Ref.20 Ref.22 Ref.24
	Modified residue	2453	1	Phosphoserine Ref.22
	Modified residue	2581	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	2583	1	Phosphothreonine Ref.22
	Modified residue	2664	1	Phosphoserine Ref.22 Ref.24
	Modified residue	2675	1	Phosphoserine Ref.17
	Modified residue	2677	1	Phosphoserine Ref.17
	Modified residue	2684	1	Phosphoserine Ref.22 Ref.24
	Modified residue	2688	1	Phosphoserine Ref.22 Ref.24
	Modified residue	2690	1	Phosphoserine Ref.17 Ref.22
	Modified residue	2692	1	Phosphoserine Ref.17 Ref.22 Ref.24
	Modified residue	2694	1	Phosphoserine Ref.13 Ref.17 Ref.22 Ref.24
	Modified residue	2702	1	Phosphoserine Ref.22 Ref.24
	Modified residue	2706	1	Phosphoserine Ref.22 Ref.24
Natural variations
	Alternative sequence	1 – 96	96	Missing in isoform 3.		VSP_020184
	Alternative sequence	394 – 407	14	PSEAS…RSPPK → SPQLFMFLKGILVF in isoform 3.		VSP_020185
	Alternative sequence	408 – 2752	2345	Missing in isoform 3.		VSP_020186
	Alternative sequence	2023 – 2440	418	Missing in isoform 2.		VSP_020187
	Natural variant	804	1	P → T. Ref.3 Corresponds to variant rs2240140 [ dbSNP | Ensembl ].		VAR_027259
	Natural variant	856	1	T → R. Corresponds to variant rs12185191 [ dbSNP | Ensembl ].		VAR_048868
	Natural variant	883	1	S → C. Corresponds to variant rs17136053 [ dbSNP | Ensembl ].		VAR_027260
Experimental info
	Sequence conflict	157	1	A → V in AAF28898. Ref.8
	Sequence conflict	178 – 179	2	SS → NN in AAF21439. Ref.2
	Sequence conflict	195	1	D → K in AAH07752. Ref.6
	Sequence conflict	314	1	G → S in AAF21439. Ref.2
	Sequence conflict	321	1	P → A in AAF21439. Ref.2
	Sequence conflict	1474	1	S → F in BAA83716. Ref.1
	Sequence conflict	1474	1	S → F in BAA83718. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 6, 2007. Version 2. Checksum: 7A5DCEB9B50AA912	FASTA	2,752	299,615
	10 20 30 40 50 60 MYNGIGLPTP RGSGTNGYVQ RNLSLVRGRR GERPDYKGEE ELRRLEAALV KRPNPDILDH 70 80 90 100 110 120 ERKRRVELRC LELEEMMEEQ GYEEQQIQEK VATFRLMLLE KDVNPGGKEE TPGQRPAVTE 130 140 150 160 170 180 THQLAELNEK KNERLRAAFG ISDSYVDGSS FDPQRRAREA KQPAPEPPKP YSLVRESSSS 190 200 210 220 230 240 RSPTPKQKKK KKKKDRGRRS ESSSPRRERK KSSKKKKHRS ESESKKRKHR SPTPKSKRKS 250 260 270 280 290 300 KDKKRKRSRS TTPAPKSRRA HRSTSADSAS SSDTSRSRSR SAAAKTHTTA LAGRSPSPAS 310 320 330 340 350 360 GRRGEGDAPF SEPGTTSTQR PSSPETATKQ PSSPYEDKDK DKKEKSATRP SPSPERSSTG 370 380 390 400 410 420 PEPPAPTPLL AERHGGSPQP LATTPLSQEP VNPPSEASPT RDRSPPKSPE KLPQSSSSES 430 440 450 460 470 480 SPPSPQPTKV SRHASSSPES PKPAPAPGSH REISSSPTSK NRSHGRAKRD KSHSHTPSRR 490 500 510 520 530 540 MGRSRSPATA KRGRSRSRTP TKRGHSRSRS PQWRRSRSAQ RWGRSRSPQR RGRSRSPQRP 550 560 570 580 590 600 GWSRSRNTQR RGRSRSARRG RSHSRSPATR GRSRSRTPAR RGRSRSRTPA RRRSRSRTPT 610 620 630 640 650 660 RRRSRSRTPA RRGRSRSRTP ARRRSRTRSP VRRRSRSRSP ARRSGRSRSR TPARRGRSRS 670 680 690 700 710 720 RTPARRGRSR SRTPARRSGR SRSRTPARRG RSRSRTPRRG RSRSRSLVRR GRSHSRTPQR 730 740 750 760 770 780 RGRSGSSSER KNKSRTSQRR SRSNSSPEMK KSRISSRRSR SLSSPRSKAK SRLSLRRSLS 790 800 810 820 830 840 GSSPCPKQKS QTPPRRSRSG SSQPKAKSRT PPRRSRSSSS PPPKQKSKTP SRQSHSSSSP 850 860 870 880 890 900 HPKVKSGTPP RQGSITSPQA NEQSVTPQRR SCFESSPDPE LKSRTPSRHS CSGSSPPRVK 910 920 930 940 950 960 SSTPPRQSPS RSSSPQPKVK AIISPRQRSH SGSSSPSPSR VTSRTTPRRS RSVSPCSNVE 970 980 990 1000 1010 1020 SRLLPRYSHS GSSSPDTKVK PETPPRQSHS GSISPYPKVK AQTPPGPSLS GSKSPCPQEK 1030 1040 1050 1060 1070 1080 SKDSLVQSCP GSLSLCAGVK SSTPPGESYF GVSSLQLKGQ SQTSPDHRSD TSSPEVRQSH 1090 1100 1110 1120 1130 1140 SESPSLQSKS QTSPKGGRSR SSSPVTELAS RSPIRQDRGE FSASPMLKSG MSPEQSRFQS 1150 1160 1170 1180 1190 1200 DSSSYPTVDS NSLLGQSRLE TAESKEKMAL PPQEDATASP PRQKDKFSPF PVQDRPESSL 1210 1220 1230 1240 1250 1260 VFKDTLRTPP RERSGAGSSP ETKEQNSALP TSSQDEELME VVEKSEEPAG QILSHLSSEL 1270 1280 1290 1300 1310 1320 KEMSTSNFES SPEVEERPAV SLTLDQSQSQ ASLEAVEVPS MASSWGGPHF SPEHKELSNS 1330 1340 1350 1360 1370 1380 PLRENSFGSP LEFRNSGPLG TEMNTGFSSE VKEDLNGPFL NQLETDPSLD MKEQSTRSSG 1390 1400 1410 1420 1430 1440 HSSSELSPDA VEKAGMSSNQ SISSPVLDAV PRTPSRERSS SASSPEMKDG LPRTPSRRSR 1450 1460 1470 1480 1490 1500 SGSSPGLRDG SGTPSRHSLS GSSPGMKDIP RTPSRGRSEC DSSPEPKALP QTPRPRSRSP 1510 1520 1530 1540 1550 1560 SSPELNNKCL TPQRERSGSE SSVDQKTVAR TPLGQRSRSG SSQELDVKPS ASPQERSESD 1570 1580 1590 1600 1610 1620 SSPDSKAKTR TPLRQRSRSG SSPEVDSKSR LSPRRSRSGS SPEVKDKPRA APRAQSGSDS 1630 1640 1650 1660 1670 1680 SPEPKAPAPR ALPRRSRSGS SSKGRGPSPE GSSSTESSPE HPPKSRTARR GSRSSPEPKT 1690 1700 1710 1720 1730 1740 KSRTPPRRRS SRSSPELTRK ARLSRRSRSA SSSPETRSRT PPRHRRSPSV SSPEPAEKSR 1750 1760 1770 1780 1790 1800 SSRRRRSASS PRTKTTSRRG RSPSPKPRGL QRSRSRSRRE KTRTTRRRDR SGSSQSTSRR 1810 1820 1830 1840 1850 1860 RQRSRSRSRV TRRRRGGSGY HSRSPARQES SRTSSRRRRG RSRTPPTSRK RSRSRTSPAP 1870 1880 1890 1900 1910 1920 WKRSRSRASP ATHRRSRSRT PLISRRRSRS RTSPVSRRRS RSRTSVTRRR SRSRASPVSR 1930 1940 1950 1960 1970 1980 RRSRSRTPPV TRRRSRSRTP TTRRRSRSRT PPVTRRRSRS RTPPVTRRRS RSRTSPITRR 1990 2000 2010 2020 2030 2040 RSRSRTSPVT RRRSRSRTSP VTRRRSRSRT SPVTRRRSRS RTPPAIRRRS RSRTPLLPRK 2050 2060 2070 2080 2090 2100 RSRSRSPLAI RRRSRSRTPR TARGKRSLTR SPPAIRRRSA SGSSSDRSRS ATPPATRNHS 2110 2120 2130 2140 2150 2160 GSRTPPVALN SSRMSCFSRP SMSPTPLDRC RSPGMLEPLG SSRTPMSVLQ QAGGSMMDGP 2170 2180 2190 2200 2210 2220 GPRIPDHQRT SVPENHAQSR IALALTAISL GTARPPPSMS AAGLAARMSQ VPAPVPLMSL 2230 2240 2250 2260 2270 2280 RTAPAANLAS RIPAASAAAM NLASARTPAI PTAVNLADSR TPAAAAAMNL ASPRTAVAPS 2290 2300 2310 2320 2330 2340 AVNLADPRTP TAPAVNLAGA RTPAALAALS LTGSGTPPTA ANYPSSSRTP QAPASANLVG 2350 2360 2370 2380 2390 2400 PRSAHATAPV NIAGSRTAAA LAPASLTSAR MAPALSGANL TSPRVPLSAY ERVSGRTSPP 2410 2420 2430 2440 2450 2460 LLDRARSRTP PSAPSQSRMT SERAPSPSSR MGQAPSQSLL PPAQDQPRSP VPSAFSDQSR 2470 2480 2490 2500 2510 2520 CLIAQTTPVA GSQSLSSGAV ATTTSSAGDH NGMLSVPAPG VPHSDVGEPP ASTGAQQPSA 2530 2540 2550 2560 2570 2580 LAALQPAKER RSSSSSSSSS SSSSSSSSSS SSSSSSGSSS SDSEGSSLPV QPEVALKRVP 2590 2600 2610 2620 2630 2640 SPTPAPKEAV REGRPPEPTP AKRKRRSSSS SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS 2650 2660 2670 2680 2690 2700 SSSSSSSSPS PAKPGPQALP KPASPKKPPP GERRSRSPRK PIDSLRDSRS LSYSPVERRR 2710 2720 2730 2740 2750 PSPQPSPRDQ QSSSSERGSR RGQRGDSRSP SHKRRRETPS PRPMRHRSSR SP
	Isoform 2 [UniParc]. Checksum: 22CE5B02DA3E03CC	FASTA	2,334	256,645
	10 20 30 40 50 60 MYNGIGLPTP RGSGTNGYVQ RNLSLVRGRR GERPDYKGEE ELRRLEAALV KRPNPDILDH 70 80 90 100 110 120 ERKRRVELRC LELEEMMEEQ GYEEQQIQEK VATFRLMLLE KDVNPGGKEE TPGQRPAVTE 130 140 150 160 170 180 THQLAELNEK KNERLRAAFG ISDSYVDGSS FDPQRRAREA KQPAPEPPKP YSLVRESSSS 190 200 210 220 230 240 RSPTPKQKKK KKKKDRGRRS ESSSPRRERK KSSKKKKHRS ESESKKRKHR SPTPKSKRKS 250 260 270 280 290 300 KDKKRKRSRS TTPAPKSRRA HRSTSADSAS SSDTSRSRSR SAAAKTHTTA LAGRSPSPAS 310 320 330 340 350 360 GRRGEGDAPF SEPGTTSTQR PSSPETATKQ PSSPYEDKDK DKKEKSATRP SPSPERSSTG 370 380 390 400 410 420 PEPPAPTPLL AERHGGSPQP LATTPLSQEP VNPPSEASPT RDRSPPKSPE KLPQSSSSES 430 440 450 460 470 480 SPPSPQPTKV SRHASSSPES PKPAPAPGSH REISSSPTSK NRSHGRAKRD KSHSHTPSRR 490 500 510 520 530 540 MGRSRSPATA KRGRSRSRTP TKRGHSRSRS PQWRRSRSAQ RWGRSRSPQR RGRSRSPQRP 550 560 570 580 590 600 GWSRSRNTQR RGRSRSARRG RSHSRSPATR GRSRSRTPAR RGRSRSRTPA RRRSRSRTPT 610 620 630 640 650 660 RRRSRSRTPA RRGRSRSRTP ARRRSRTRSP VRRRSRSRSP ARRSGRSRSR TPARRGRSRS 670 680 690 700 710 720 RTPARRGRSR SRTPARRSGR SRSRTPARRG RSRSRTPRRG RSRSRSLVRR GRSHSRTPQR 730 740 750 760 770 780 RGRSGSSSER KNKSRTSQRR SRSNSSPEMK KSRISSRRSR SLSSPRSKAK SRLSLRRSLS 790 800 810 820 830 840 GSSPCPKQKS QTPPRRSRSG SSQPKAKSRT PPRRSRSSSS PPPKQKSKTP SRQSHSSSSP 850 860 870 880 890 900 HPKVKSGTPP RQGSITSPQA NEQSVTPQRR SCFESSPDPE LKSRTPSRHS CSGSSPPRVK 910 920 930 940 950 960 SSTPPRQSPS RSSSPQPKVK AIISPRQRSH SGSSSPSPSR VTSRTTPRRS RSVSPCSNVE 970 980 990 1000 1010 1020 SRLLPRYSHS GSSSPDTKVK PETPPRQSHS GSISPYPKVK AQTPPGPSLS GSKSPCPQEK 1030 1040 1050 1060 1070 1080 SKDSLVQSCP GSLSLCAGVK SSTPPGESYF GVSSLQLKGQ SQTSPDHRSD TSSPEVRQSH 1090 1100 1110 1120 1130 1140 SESPSLQSKS QTSPKGGRSR SSSPVTELAS RSPIRQDRGE FSASPMLKSG MSPEQSRFQS 1150 1160 1170 1180 1190 1200 DSSSYPTVDS NSLLGQSRLE TAESKEKMAL PPQEDATASP PRQKDKFSPF PVQDRPESSL 1210 1220 1230 1240 1250 1260 VFKDTLRTPP RERSGAGSSP ETKEQNSALP TSSQDEELME VVEKSEEPAG QILSHLSSEL 1270 1280 1290 1300 1310 1320 KEMSTSNFES SPEVEERPAV SLTLDQSQSQ ASLEAVEVPS MASSWGGPHF SPEHKELSNS 1330 1340 1350 1360 1370 1380 PLRENSFGSP LEFRNSGPLG TEMNTGFSSE VKEDLNGPFL NQLETDPSLD MKEQSTRSSG 1390 1400 1410 1420 1430 1440 HSSSELSPDA VEKAGMSSNQ SISSPVLDAV PRTPSRERSS SASSPEMKDG LPRTPSRRSR 1450 1460 1470 1480 1490 1500 SGSSPGLRDG SGTPSRHSLS GSSPGMKDIP RTPSRGRSEC DSSPEPKALP QTPRPRSRSP 1510 1520 1530 1540 1550 1560 SSPELNNKCL TPQRERSGSE SSVDQKTVAR TPLGQRSRSG SSQELDVKPS ASPQERSESD 1570 1580 1590 1600 1610 1620 SSPDSKAKTR TPLRQRSRSG SSPEVDSKSR LSPRRSRSGS SPEVKDKPRA APRAQSGSDS 1630 1640 1650 1660 1670 1680 SPEPKAPAPR ALPRRSRSGS SSKGRGPSPE GSSSTESSPE HPPKSRTARR GSRSSPEPKT 1690 1700 1710 1720 1730 1740 KSRTPPRRRS SRSSPELTRK ARLSRRSRSA SSSPETRSRT PPRHRRSPSV SSPEPAEKSR 1750 1760 1770 1780 1790 1800 SSRRRRSASS PRTKTTSRRG RSPSPKPRGL QRSRSRSRRE KTRTTRRRDR SGSSQSTSRR 1810 1820 1830 1840 1850 1860 RQRSRSRSRV TRRRRGGSGY HSRSPARQES SRTSSRRRRG RSRTPPTSRK RSRSRTSPAP 1870 1880 1890 1900 1910 1920 WKRSRSRASP ATHRRSRSRT PLISRRRSRS RTSPVSRRRS RSRTSVTRRR SRSRASPVSR 1930 1940 1950 1960 1970 1980 RRSRSRTPPV TRRRSRSRTP TTRRRSRSRT PPVTRRRSRS RTPPVTRRRS RSRTSPITRR 1990 2000 2010 2020 2030 2040 RSRSRTSPVT RRRSRSRTSP VTRRRSRSRT SPVTRRRSRS RTPPAQDQPR SPVPSAFSDQ 2050 2060 2070 2080 2090 2100 SRCLIAQTTP VAGSQSLSSG AVATTTSSAG DHNGMLSVPA PGVPHSDVGE PPASTGAQQP 2110 2120 2130 2140 2150 2160 SALAALQPAK ERRSSSSSSS SSSSSSSSSS SSSSSSSSGS SSSDSEGSSL PVQPEVALKR 2170 2180 2190 2200 2210 2220 VPSPTPAPKE AVREGRPPEP TPAKRKRRSS SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS 2230 2240 2250 2260 2270 2280 SSSSSSSSSS PSPAKPGPQA LPKPASPKKP PPGERRSRSP RKPIDSLRDS RSLSYSPVER 2290 2300 2310 2320 2330 RRPSPQPSPR DQQSSSSERG SRRGQRGDSR SPSHKRRRET PSPRPMRHRS SRSP
	Isoform 3 [UniParc]. Checksum: F8391BC3C125F65B	FASTA	311	34,212
	10 20 30 40 50 60 MLLEKDVNPG GKEETPGQRP AVTETHQLAE LNEKKNERLR AAFGISDSYV DGSSFDPQRR 70 80 90 100 110 120 AREAKQPAPE PPKPYSLVRE SSSSRSPTPK QKKKKKKKDR GRRSESSSPR RERKKSSKKK 130 140 150 160 170 180 KHRSESESKK RKHRSPTPKS KRKSKDKKRK RSRSTTPAPK SRRAHRSTSA DSASSSDTSR 190 200 210 220 230 240 SRSRSAAAKT HTTALAGRSP SPASGRRGEG DAPFSEPGTT STQRPSSPET ATKQPSSPYE 250 260 270 280 290 300 DKDKDKKEKS ATRPSPSPER SSTGPEPPAP TPLLAERHGG SPQPLATTPL SQEPVNPSPQ 310 LFMFLKGILV F

References

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[1]	"Cloning and characterization of a novel RNA-binding protein SRL300 with RS domains." Sawada Y., Miura Y., Umeki K., Tamaoki T., Fujinaga K., Ohtaki S. Biochim. Biophys. Acta 1492:191-195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, TISSUE SPECIFICITY, PHOSPHORYLATION. Tissue: Cervix carcinoma.
[2]	"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 1223-1226 AND 2587-2597, FUNCTION.
[3]	"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-804. Tissue: Brain.
[4]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1018 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2555-2752 (ISOFORMS 1/2). Tissue: Embryonic testis, Muscle, Placenta and Retina.
[7]	Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-11; 44-51; 116-130; 137-155; 357-401; 1001-1013; 1041-1058; 1101-1111; 1119-1128; 1138-1158; 1224-1277; 1316-1352; 1394-1412; 1539-1556; 2104-2113; 2120-2129; 2132-2163; 2181-2221; 2232-2392; 2431-2460 AND 2690-2698, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[8]	"Human partial CDS from CD34+ stem cells." Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-185. Tissue: Umbilical cord blood.
[9]	"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: IDENTIFICATION IN A PRE-MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRP70; SNRPA1 AND SRRM1.
[10]	"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.
[11]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[12]	"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 SER-440; THR-1003; SER-1132; SER-1188; SER-1329 AND THR-1492, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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 THR-367; SER-377; SER-871; SER-876; SER-954; SER-1072; SER-1073; SER-1102; SER-2272; THR-2291; THR-2316; SER-2382 AND SER-2694, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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 THR-1531, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-2449, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2272, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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 SER-295; SER-297; SER-322; SER-323; SER-351; SER-353; SER-377; SER-387; SER-398; SER-435; SER-440; SER-778; SER-780; SER-783; SER-857; SER-864; THR-866; SER-950; SER-952; SER-954; SER-957; SER-968; SER-970; SER-972; SER-974; THR-983; SER-994; THR-1003; SER-1014; SER-1028; SER-1032; SER-1064; SER-1069; SER-1072; SER-1073; SER-1099; SER-1101; SER-1102; SER-1103; SER-1112; SER-1179; SER-1188; THR-1208; SER-1318; SER-1320; SER-1326; SER-1329; SER-1387; SER-1401; SER-1404; THR-1413; SER-1415; SER-1444; SER-1451; THR-1453; THR-1472; THR-1511; SER-1522; THR-1531; SER-1537; SER-1539; SER-1541; SER-1542; SER-1552; SER-1691; SER-1693; SER-1694; THR-1698; SER-1876; SER-1878; THR-1880; SER-1923; SER-1925; THR-1927; SER-1946; SER-1948; THR-1950; SER-1958; SER-1960; THR-1962; SER-1970; SER-2100; SER-2102; THR-2104; SER-2118; SER-2121; SER-2123; SER-2132; THR-2144; SER-2272; THR-2289; THR-2302; THR-2316; THR-2329; SER-2382; SER-2398; SER-2407; THR-2409; SER-2412; SER-2449; SER-2581; SER-2675; SER-2677; SER-2690; SER-2692 AND SER-2694, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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].
[19]	"Physical and genetic interactions of yeast Cwc21p, an ortholog of human SRm300/SRRM2, suggest a role at the catalytic center of the spliceosome." Grainger R.J., Barrass J.D., Jacquier A., Rain J.-C., Beggs J.D. RNA 15:2161-2173(2009) [PubMed] [Europe PMC] [Abstract] Cited for: COMPLEMENTATION OF YEAST MUTANTS.
[20]	"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 TYR-145; SER-322; SER-323; SER-351; SER-353; SER-357; SER-358; THR-359; THR-367; SER-377; SER-846; SER-857; THR-866; SER-876; SER-952; SER-954; THR-1003; SER-1099; SER-1101; SER-1102; SER-1103; THR-1106; SER-1214; SER-1318; SER-1320; SER-1326; SER-1329; SER-1382; SER-1387; SER-1401; SER-1403; SER-1404; SER-2100; SER-2102; THR-2104; SER-2132; SER-2272; THR-2289; THR-2316; THR-2381; SER-2382 AND SER-2449, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"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-169, MASS SPECTROMETRY.
[22]	"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 SER-220; SER-222; THR-286; SER-295; SER-297; SER-300; SER-351; SER-353; THR-367; SER-377; SER-424; SER-440; SER-454; SER-484; SER-486; SER-778; THR-866; SER-871; SER-875; SER-876; SER-950; SER-973; SER-974; THR-983; SER-994; THR-1003; SER-1014; SER-1028; SER-1083; SER-1099; SER-1101; SER-1103; SER-1122; SER-1124; SER-1132; SER-1152; SER-1179; SER-1188; SER-1219; SER-1320; SER-1326; SER-1329; SER-1336; SER-1368; SER-1387; SER-1404; THR-1413; SER-1415; SER-1421; THR-1434; SER-1460; SER-1462; SER-1463; SER-1482; SER-1483; THR-1492; SER-1497; SER-1499; SER-1501; SER-1502; SER-1621; SER-1762; SER-1764; SER-1854; SER-1857; SER-1890; THR-1892; SER-1893; SER-1916; SER-1919; SER-1925; THR-1927; SER-1948; THR-1950; SER-1960; THR-1962; SER-1972; SER-1975; SER-1984; SER-1987; SER-1996; SER-1999; SER-2008; SER-2011; SER-2044; SER-2046; THR-2069; SER-2071; SER-2102; THR-2104; SER-2123; SER-2132; SER-2272; THR-2289; THR-2302; THR-2329; SER-2335; SER-2343; SER-2382; SER-2394; SER-2398; SER-2407; THR-2409; SER-2449; SER-2453; SER-2581; THR-2583; SER-2664; SER-2684; SER-2688; SER-2690; SER-2692; SER-2694; SER-2702 AND SER-2706, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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].
[24]	"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 SER-297; SER-333; SER-351; SER-353; SER-377; SER-398; SER-404; SER-408; SER-424; SER-440; SER-778; SER-783; SER-876; SER-908; SER-973; SER-974; THR-977; SER-992; THR-1003; THR-1043; SER-1069; SER-1083; SER-1099; SER-1101; SER-1103; SER-1124; SER-1129; SER-1132; SER-1179; SER-1188; SER-1219; SER-1320; SER-1329; SER-1382; SER-1387; SER-1404; THR-1413; SER-1415; SER-1424; SER-1444; SER-1458; SER-1463; SER-1497; SER-1499; SER-1502; SER-1517; SER-1519; SER-1521; SER-1522; SER-1542; SER-1552; SER-1577; SER-1579; SER-1581; SER-1582; SER-1598; SER-1600; SER-1601; SER-1648; SER-1658; SER-1694; SER-1727; SER-1729; SER-1731; SER-1732; SER-1762; SER-1764; SER-1818; SER-1822; SER-1854; SER-1878; SER-1884; SER-1890; SER-1916; SER-1919; SER-1925; THR-1927; THR-1931; SER-1948; THR-1950; THR-1954; SER-1960; THR-1962; THR-1966; SER-1970; SER-1972; SER-1975; THR-1978; SER-1984; SER-1987; SER-1996; SER-1999; SER-2008; SER-2011; SER-2020; THR-2022; SER-2032; THR-2034; SER-2044; SER-2046; SER-2067; THR-2069; SER-2071; SER-2090; THR-2092; THR-2104; SER-2123; SER-2132; SER-2272; SER-2382; SER-2398; SER-2407; SER-2412; SER-2415; SER-2426; SER-2429; SER-2449; SER-2581; SER-2664; SER-2684; SER-2688; SER-2692; SER-2694; SER-2702 AND SER-2706, MASS SPECTROMETRY.
[25]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB015644 mRNA. Translation: BAA34957.1. AB016087 mRNA. Translation: BAA83713.1. AB016089 mRNA. Translation: BAA83715.1. AB016090 mRNA. Translation: BAA83716.1. AB016091 mRNA. Translation: BAA83717.1. AB016092 mRNA. Translation: BAA83718.1. AF201422 mRNA. Translation: AAF21439.1. Frameshift. AB002322 mRNA. Translation: BAA20782.3. Different initiation. AC092117 Genomic DNA. No translation available. CH471112 Genomic DNA. Translation: EAW85478.1. CH471112 Genomic DNA. Translation: EAW85477.1. CH471112 Genomic DNA. Translation: EAW85480.1. BC007752 mRNA. Translation: AAH07752.1. BC009062 mRNA. Translation: AAH09062.1. BC041155 mRNA. Translation: AAH41155.1. BC070050 mRNA. Translation: AAH70050.1. Sequence problems. AF161338 mRNA. Translation: AAF28898.1. Frameshift.
IPI	IPI00782992. IPI00784560. IPI00785023.
RefSeq	NP_057417.3. NM_016333.3. XP_005255282.1. XM_005255225.1.
UniGene	Hs.433343.
3D structure databases
ProteinModelPortal	Q9UQ35.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UQ35. 46 interactions.
MINT	MINT-5006711.
PTM databases
PhosphoSite	Q9UQ35.
Polymorphism databases
DMDM	143928063.
Proteomic databases
PaxDb	Q9UQ35.
PRIDE	Q9UQ35.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000301740; ENSP00000301740; ENSG00000167978.
GeneID	23524.
KEGG	hsa:23524.
UCSC	uc002crj.1. human.
Organism-specific databases
CTD	23524.
GeneCards	GC16P002769.
H-InvDB	HIX0194349.
HGNC	HGNC:16639. SRRM2.
HPA	HPA041411.
MIM	606032. gene.
neXtProt	NX_Q9UQ35.
PharmGKB	PA38178.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOVERGEN	HBG093999.
InParanoid	Q9UQ35.
KO	K13172.
OMA	CFSRPSM.
OrthoDB	EOG70W3CH.
PhylomeDB	Q9UQ35.
Gene expression databases
ArrayExpress	Q9UQ35.
Bgee	Q9UQ35.
Genevestigator	Q9UQ35.
Family and domain databases
InterPro	IPR013170. mRNA_splic_Cwf21. IPR024945. Spt5_C_dom. [Graphical view]
Pfam	PF08312. cwf21. 1 hit. [Graphical view]
SMART	SM01104. CTD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SRRM2. human.
GeneWiki	SRRM2.
GenomeRNAi	23524.
NextBio	45984.
PRO	Q9UQ35.
SOURCE	Search...

Entry information

Entry name

SRRM2_HUMAN

Accession

Primary (citable) accession number: Q9UQ35
Secondary accession number(s): A6NKB9 , D3DU97, O15038, O94803, Q6NSL3, Q6PIM3, Q6PK40, Q8IW17, Q96GY7, Q9P0G1, Q9UHA8, Q9UQ36, Q9UQ37, Q9UQ38, Q9UQ40

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	March 6, 2007
Last modified:	November 13, 2013
This is version 109 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.