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Protein

Serine/arginine repetitive matrix protein 2

Gene

Srrm2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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. Binds to RNA (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine repetitive matrix protein 2
Gene namesi
Name:Srrm2
Synonyms:Kiaa0324
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1923206. Srrm2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27032703Serine/arginine repetitive matrix protein 2PRO_0000248155Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei101 – 1011N6-acetyllysineCombined sources
Modified residuei145 – 1451PhosphotyrosineBy similarity
Modified residuei169 – 1691N6-acetyllysineBy similarity
Modified residuei220 – 2201PhosphoserineBy similarity
Modified residuei222 – 2221PhosphoserineBy similarity
Modified residuei295 – 2951PhosphoserineCombined sources
Modified residuei300 – 3001PhosphoserineBy similarity
Modified residuei310 – 3101PhosphoserineCombined sources
Modified residuei322 – 3221PhosphoserineBy similarity
Modified residuei323 – 3231PhosphoserineCombined sources
Modified residuei349 – 3491PhosphoserineCombined sources
Modified residuei351 – 3511PhosphoserineCombined sources
Modified residuei355 – 3551PhosphoserineBy similarity
Modified residuei356 – 3561PhosphoserineBy similarity
Modified residuei357 – 3571PhosphothreonineBy similarity
Modified residuei365 – 3651PhosphothreonineBy similarity
Modified residuei375 – 3751PhosphoserineBy similarity
Modified residuei385 – 3851PhosphoserineBy similarity
Modified residuei393 – 3931PhosphoserineBy similarity
Modified residuei396 – 3961PhosphoserineBy similarity
Modified residuei402 – 4021PhosphoserineCombined sources
Modified residuei406 – 4061PhosphoserineCombined sources
Modified residuei422 – 4221PhosphoserineCombined sources
Modified residuei433 – 4331PhosphoserineCombined sources
Modified residuei434 – 4341PhosphoserineCombined sources
Modified residuei435 – 4351PhosphoserineCombined sources
Modified residuei438 – 4381PhosphoserineCombined sources
Modified residuei452 – 4521PhosphoserineBy similarity
Modified residuei482 – 4821PhosphoserineBy similarity
Modified residuei484 – 4841PhosphoserineBy similarity
Modified residuei531 – 5311PhosphoserineCombined sources
Modified residuei533 – 5331PhosphoserineCombined sources
Modified residuei773 – 7731PhosphoserineCombined sources
Modified residuei775 – 7751PhosphoserineCombined sources
Modified residuei778 – 7781PhosphoserineCombined sources
Modified residuei821 – 8211PhosphoserineBy similarity
Modified residuei829 – 8291PhosphoserineCombined sources
Modified residuei831 – 8311PhosphothreonineCombined sources
Modified residuei841 – 8411PhosphothreonineCombined sources
Modified residuei846 – 8461PhosphoserineBy similarity
Modified residuei850 – 8501PhosphoserineBy similarity
Modified residuei851 – 8511PhosphoserineBy similarity
Modified residuei882 – 8821PhosphoserineCombined sources
Modified residuei898 – 8981PhosphoserineBy similarity
Modified residuei909 – 9091PhosphoserineBy similarity
Modified residuei926 – 9261PhosphoserineBy similarity
Modified residuei928 – 9281PhosphoserineBy similarity
Modified residuei940 – 9401PhosphoserineBy similarity
Modified residuei942 – 9421PhosphoserineBy similarity
Modified residuei944 – 9441PhosphoserineBy similarity
Modified residuei945 – 9451PhosphoserineBy similarity
Modified residuei946 – 9461PhosphoserineCombined sources
Modified residuei949 – 9491PhosphoserineCombined sources
Modified residuei955 – 9551PhosphothreonineCombined sources
Modified residuei964 – 9641PhosphoserineBy similarity
Modified residuei966 – 9661PhosphotyrosineBy similarity
Modified residuei973 – 9731PhosphothreonineCombined sources
Modified residuei980 – 9801PhosphoserineBy similarity
Modified residuei984 – 9841PhosphoserineCombined sources
Modified residuei993 – 9931PhosphoserineCombined sources
Modified residuei995 – 9951PhosphothreonineCombined sources
Modified residuei997 – 9971PhosphoserineBy similarity
Modified residuei1000 – 10001PhosphoserineBy similarity
Modified residuei1011 – 10111PhosphoserineCombined sources
Modified residuei1037 – 10371PhosphoserineBy similarity
Modified residuei1038 – 10381PhosphoserineCombined sources
Modified residuei1044 – 10441PhosphothreonineCombined sources
Modified residuei1048 – 10481PhosphoserineCombined sources
Modified residuei1064 – 10641PhosphoserineBy similarity
Modified residuei1066 – 10661PhosphoserineBy similarity
Modified residuei1067 – 10671PhosphoserineCombined sources
Modified residuei1068 – 10681PhosphoserineCombined sources
Modified residuei1071 – 10711PhosphothreonineCombined sources
Modified residuei1077 – 10771PhosphoserineCombined sources
Modified residuei1087 – 10871PhosphoserineBy similarity
Modified residuei1094 – 10941PhosphoserineBy similarity
Modified residuei1097 – 10971PhosphoserineCombined sources
Modified residuei1117 – 11171PhosphoserineBy similarity
Modified residuei1151 – 11511PhosphoserineCombined sources
Modified residuei1175 – 11751PhosphoserineBy similarity
Modified residuei1216 – 12161PhosphoserineCombined sources
Modified residuei1225 – 12251PhosphoserineCombined sources
Modified residuei1229 – 12291PhosphoserineCombined sources
Modified residuei1230 – 12301PhosphoserineCombined sources
Modified residuei1269 – 12691PhosphoserineCombined sources
Modified residuei1276 – 12761PhosphoserineBy similarity
Modified residuei1278 – 12781PhosphoserineBy similarity
Modified residuei1284 – 12841PhosphoserineBy similarity
Modified residuei1287 – 12871PhosphoserineBy similarity
Modified residuei1294 – 12941PhosphoserineBy similarity
Modified residuei1305 – 13051PhosphoserineCombined sources
Modified residuei1325 – 13251PhosphoserineBy similarity
Modified residuei1338 – 13381PhosphoserineCombined sources
Modified residuei1339 – 13391PhosphoserineCombined sources
Modified residuei1340 – 13401PhosphoserineCombined sources
Modified residuei1343 – 13431PhosphoserineCombined sources
Modified residuei1359 – 13591PhosphoserineBy similarity
Modified residuei1360 – 13601PhosphoserineCombined sources
Modified residuei1370 – 13701PhosphothreonineBy similarity
Modified residuei1372 – 13721PhosphoserineBy similarity
Modified residuei1378 – 13781PhosphoserineBy similarity
Modified residuei1380 – 13801PhosphoserineCombined sources
Modified residuei1390 – 13901PhosphothreonineBy similarity
Modified residuei1400 – 14001PhosphoserineCombined sources
Modified residuei1407 – 14071PhosphoserineBy similarity
Modified residuei1409 – 14091PhosphothreonineBy similarity
Modified residuei1414 – 14141PhosphoserineBy similarity
Modified residuei1416 – 14161PhosphoserineBy similarity
Modified residuei1418 – 14181PhosphoserineBy similarity
Modified residuei1419 – 14191PhosphoserineBy similarity
Modified residuei1428 – 14281PhosphothreonineCombined sources
Modified residuei1438 – 14381PhosphoserineBy similarity
Modified residuei1439 – 14391PhosphoserineBy similarity
Modified residuei1448 – 14481PhosphothreonineBy similarity
Modified residuei1453 – 14531PhosphoserineBy similarity
Modified residuei1455 – 14551PhosphoserineBy similarity
Modified residuei1457 – 14571PhosphoserineBy similarity
Modified residuei1458 – 14581PhosphoserineBy similarity
Modified residuei1465 – 14651PhosphoserineCombined sources
Modified residuei1467 – 14671PhosphothreonineCombined sources
Modified residuei1473 – 14731PhosphoserineBy similarity
Modified residuei1475 – 14751PhosphoserineBy similarity
Modified residuei1477 – 14771PhosphoserineBy similarity
Modified residuei1478 – 14781PhosphoserineBy similarity
Modified residuei1487 – 14871PhosphothreonineBy similarity
Modified residuei1493 – 14931PhosphoserineBy similarity
Modified residuei1495 – 14951PhosphoserineBy similarity
Modified residuei1497 – 14971PhosphoserineBy similarity
Modified residuei1498 – 14981PhosphoserineBy similarity
Modified residuei1508 – 15081PhosphoserineCombined sources
Modified residuei1533 – 15331PhosphoserineBy similarity
Modified residuei1535 – 15351PhosphoserineBy similarity
Modified residuei1537 – 15371PhosphoserineBy similarity
Modified residuei1538 – 15381PhosphoserineBy similarity
Modified residuei1554 – 15541PhosphoserineBy similarity
Modified residuei1556 – 15561PhosphoserineBy similarity
Modified residuei1557 – 15571PhosphoserineBy similarity
Modified residuei1572 – 15721PhosphoserineCombined sources
Modified residuei1576 – 15761PhosphoserineCombined sources
Modified residuei1577 – 15771PhosphoserineCombined sources
Modified residuei1604 – 16041PhosphoserineBy similarity
Modified residuei1614 – 16141PhosphoserineBy similarity
Modified residuei1647 – 16471PhosphoserineBy similarity
Modified residuei1649 – 16491PhosphoserineBy similarity
Modified residuei1650 – 16501PhosphoserineBy similarity
Modified residuei1654 – 16541PhosphothreonineBy similarity
Modified residuei1683 – 16831PhosphoserineBy similarity
Modified residuei1685 – 16851PhosphoserineBy similarity
Modified residuei1687 – 16871PhosphoserineBy similarity
Modified residuei1688 – 16881PhosphoserineBy similarity
Modified residuei1718 – 17181PhosphoserineBy similarity
Modified residuei1720 – 17201PhosphoserineBy similarity
Modified residuei1774 – 17741PhosphoserineBy similarity
Modified residuei1778 – 17781PhosphoserineBy similarity
Modified residuei1810 – 18101PhosphoserineBy similarity
Modified residuei1813 – 18131PhosphoserineCombined sources
Modified residuei1832 – 18321PhosphoserineBy similarity
Modified residuei1834 – 18341PhosphoserineBy similarity
Modified residuei1836 – 18361PhosphothreonineBy similarity
Modified residuei1840 – 18401PhosphoserineBy similarity
Modified residuei1846 – 18461PhosphoserineBy similarity
Modified residuei1848 – 18481PhosphothreonineBy similarity
Modified residuei1849 – 18491PhosphoserineBy similarity
Modified residuei1869 – 18691PhosphoserineBy similarity
Modified residuei1872 – 18721PhosphoserineBy similarity
Modified residuei1876 – 18761PhosphoserineBy similarity
Modified residuei1878 – 18781PhosphoserineBy similarity
Modified residuei1880 – 18801PhosphothreonineBy similarity
Modified residuei1884 – 18841PhosphothreonineBy similarity
Modified residuei1898 – 18981PhosphoserineBy similarity
Modified residuei1900 – 19001PhosphoserineBy similarity
Modified residuei1902 – 19021PhosphothreonineBy similarity
Modified residuei1906 – 19061PhosphothreonineBy similarity
Modified residuei1910 – 19101PhosphoserineBy similarity
Modified residuei1912 – 19121PhosphoserineBy similarity
Modified residuei1914 – 19141PhosphothreonineBy similarity
Modified residuei1918 – 19181PhosphothreonineBy similarity
Modified residuei1922 – 19221PhosphoserineBy similarity
Modified residuei1924 – 19241PhosphoserineBy similarity
Modified residuei1927 – 19271PhosphoserineBy similarity
Modified residuei1930 – 19301PhosphothreonineBy similarity
Modified residuei1936 – 19361PhosphoserineBy similarity
Modified residuei1939 – 19391PhosphoserineBy similarity
Modified residuei1948 – 19481PhosphoserineBy similarity
Modified residuei1951 – 19511PhosphoserineBy similarity
Modified residuei1960 – 19601PhosphoserineBy similarity
Modified residuei1963 – 19631PhosphoserineBy similarity
Modified residuei1972 – 19721PhosphoserineBy similarity
Modified residuei1974 – 19741PhosphothreonineBy similarity
Modified residuei1982 – 19821PhosphoserineCombined sources
Modified residuei1984 – 19841PhosphoserineCombined sources
Modified residuei1986 – 19861PhosphothreonineCombined sources
Modified residuei1996 – 19961PhosphoserineBy similarity
Modified residuei1998 – 19981PhosphoserineBy similarity
Modified residuei2019 – 20191PhosphoserineBy similarity
Modified residuei2021 – 20211PhosphothreonineBy similarity
Modified residuei2023 – 20231PhosphoserineBy similarity
Modified residuei2042 – 20421PhosphoserineBy similarity
Modified residuei2044 – 20441PhosphothreonineBy similarity
Modified residuei2052 – 20521PhosphoserineCombined sources
Modified residuei2054 – 20541PhosphoserineCombined sources
Modified residuei2056 – 20561PhosphothreonineCombined sources
Modified residuei2070 – 20701PhosphoserineCombined sources
Modified residuei2073 – 20731PhosphoserineCombined sources
Modified residuei2075 – 20751PhosphoserineCombined sources
Modified residuei2084 – 20841PhosphoserineCombined sources
Modified residuei2096 – 20961PhosphothreonineBy similarity
Modified residuei2224 – 22241PhosphoserineCombined sources
Modified residuei2241 – 22411PhosphothreonineBy similarity
Modified residuei2254 – 22541PhosphothreonineBy similarity
Modified residuei2268 – 22681PhosphothreonineBy similarity
Modified residuei2281 – 22811PhosphothreonineBy similarity
Modified residuei2296 – 22961PhosphoserineBy similarity
Modified residuei2334 – 23341PhosphothreonineBy similarity
Modified residuei2335 – 23351PhosphoserineCombined sources
Modified residuei2347 – 23471PhosphoserineBy similarity
Modified residuei2351 – 23511PhosphoserineCombined sources
Modified residuei2360 – 23601PhosphoserineBy similarity
Modified residuei2362 – 23621PhosphothreonineBy similarity
Modified residuei2365 – 23651PhosphoserineBy similarity
Modified residuei2368 – 23681PhosphoserineBy similarity
Modified residuei2381 – 23811PhosphoserineCombined sources
Modified residuei2384 – 23841PhosphoserineBy similarity
Modified residuei2404 – 24041PhosphoserineCombined sources
Modified residuei2408 – 24081PhosphoserineBy similarity
Modified residuei2535 – 25351PhosphoserineCombined sources
Modified residuei2537 – 25371PhosphothreonineBy similarity
Modified residuei2618 – 26181PhosphoserineBy similarity
Modified residuei2629 – 26291PhosphoserineBy similarity
Modified residuei2631 – 26311PhosphoserineBy similarity
Modified residuei2638 – 26381PhosphoserineBy similarity
Modified residuei2642 – 26421PhosphoserineBy similarity
Modified residuei2644 – 26441PhosphoserineBy similarity
Modified residuei2646 – 26461PhosphoserineCombined sources
Modified residuei2648 – 26481PhosphoserineCombined sources
Modified residuei2656 – 26561PhosphoserineCombined sources
Modified residuei2660 – 26601PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BTI8.
MaxQBiQ8BTI8.
PaxDbiQ8BTI8.
PRIDEiQ8BTI8.

2D gel databases

REPRODUCTION-2DPAGEIPI00225062.
IPI00785240.

PTM databases

iPTMnetiQ8BTI8.
PhosphoSiteiQ8BTI8.

Expressioni

Gene expression databases

BgeeiQ8BTI8.
CleanExiMM_SRRM2.
ExpressionAtlasiQ8BTI8. baseline and differential.
GenevisibleiQ8BTI8. MM.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi217871. 4 interactions.
IntActiQ8BTI8. 2 interactions.
MINTiMINT-4112373.
STRINGi10090.ENSMUSP00000085993.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni197 – 25963Sufficient for RNA-bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili60 – 9233Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi186 – 24661Lys-richAdd
BLAST
Compositional biasi200 – 27022503Ser-richAdd
BLAST
Compositional biasi348 – 44598Pro-richAdd
BLAST
Compositional biasi478 – 772295Arg-richAdd
BLAST
Compositional biasi1622 – 2041420Arg-richAdd
BLAST
Compositional biasi2134 – 2260127Ala-richAdd
BLAST

Sequence similaritiesi

Belongs to the CWC21 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1869. Eukaryota.
ENOG4111F3M. LUCA.
GeneTreeiENSGT00730000110977.
HOGENOMiHOG000154424.
HOVERGENiHBG093999.
InParanoidiQ8BTI8.
KOiK13172.
OMAiPEMKKSH.
OrthoDBiEOG70W3CH.
TreeFamiTF335721.

Family and domain databases

InterProiIPR013170. mRNA_splic_Cwf21_dom.
IPR024945. Spt5_C_dom.
[Graphical view]
PfamiPF08312. cwf21. 1 hit.
[Graphical view]
SMARTiSM01104. CTD. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BTI8-1) [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
MYNGIGLPTP RGSGTNGYVQ RNLSLVRGRR GERPDYKGEE ELRHLEAALV
60 70 80 90 100
KRPNPDILDH ERKRRVELRC LELEEMMEEQ GYEEQQIQEK VATFRLMLLE
110 120 130 140 150
KDVNPGAKEE TPGQRPVVTE THQLAELNEK KNERLRAAFG ISDSYVDGSS
160 170 180 190 200
FDPQRRAREA KQIAPEPPKP YSLVRETSSS RSPTPKQKKK KKKKDRGRRS
210 220 230 240 250
ESSSPRRERK KSSKKKKHRS ESESKKRKHR SPTPKSKRKS KDKKRKRSRS
260 270 280 290 300
TTPAPKSRRA HRSTSADSAS SSDTSRSRSR SAAAKIHTTA LTGQSPPLAS
310 320 330 340 350
GHQGEGDAPS VEPGATNIQQ PSSPAPSTKQ SSSPYEDKDK KEKSAVRPSP
360 370 380 390 400
SPERSSTGPE LPAPTPLLVE QHVDSPRPLA AIPSSQEPVN PSSEASPTRG
410 420 430 440 450
CSPPKSPEKP PQSTSSESCP PSPQPTKGSR HASSSPESLK PTPAPGSRRE
460 470 480 490 500
ISSSPTSKNR SHGRAKRDKS HSHTPSHRAG RSRSPATKRG RSRSRTPTKR
510 520 530 540 550
GHSRSRSPQW RRSRSAQRWG KSRSPQRRGR SRSPQRPGWS RSRNTQRRGR
560 570 580 590 600
SRSARRGRSH SRSPATRGRS RSRTPARRGR SRSRTPARRR SRSRTPARRR
610 620 630 640 650
SRSRTPARRG RSRSRTPARR RSRTRSPVRR RSRSRSQARR SGRSRSRTPA
660 670 680 690 700
RRSGRSRSRT PARRGRSRSR TPARRSARSR SRTPARRGRS RSRTPARRRS
710 720 730 740 750
RSRSLVRRGR SHSRTPQRRG RSGSSSERKN KSRTSQRRSR SNSSPEMKKS
760 770 780 790 800
HVSSRRSRSL SSPRSKAKSL RRSLSGSSPC PKQKSQTPTR RSRSGSSPPK
810 820 830 840 850
QKSKTPPRQS RSNSPQPKVK SGTPPRPGSV TNMQADECTA TPQRQSHSES
860 870 880 890 900
SPDGEVKSRT PSRQSCSGSS PRVKSSTPPR QSPSRSSSPQ PKVKTVISPR
910 920 930 940 950
GRSHSSSSSP SPSRVTSRTP QRKSRSISPC PKVDSRLRHS RSRSSSPDSK
960 970 980 990 1000
MELGTPLRHS GSTSPYLKSM LQTPPDQNLS GSKSPCPQKS RDSPTGSSGS
1010 1020 1030 1040 1050
FHLCPGVTPS SIVPGESCFS ASFVQQKGHT QTWPDTSSPE VMQTQVESPL
1060 1070 1080 1090 1100
LQSKSQTSPK GSLSRSSSPV TELTARSPVK QDKSEISTDP KLKSGMSPEQ
1110 1120 1130 1140 1150
SKTKPDSSIY PLVDSKSFLV QSRLEPSELK ERLGLIQEDV ASSCIPRDKF
1160 1170 1180 1190 1200
SPTQDRPESS TVLKVTPRVL LKERSGAGSP PGKRDQKSLL PNSSQDELME
1210 1220 1230 1240 1250
VEKSEQPLSQ VLPSLSPEHK EMPGSNIESS PEVEERPAVL SALDQSQSQP
1260 1270 1280 1290 1300
SKAAETPAVA SCWSGPQVSP EHKELSHSPP RENSFESSLE FKNSGPVSEV
1310 1320 1330 1340 1350
NTGFSPEVKE ELNGSFLNQT EADPSVDMKE QSRSSRRSSS ELSPEVVEKV
1360 1370 1380 1390 1400
GLFSSQKVSS PVLETVQQRT PSRERSSSAS PELKDGLPRT PSRRSRSGSS
1410 1420 1430 1440 1450
PGLRDGSGTP SRHSLSGSSP GMKDTPQTPS RGRSECDSSP EPKALPQTPR
1460 1470 1480 1490 1500
ARSHSPSSPE RNNKSVTPQR ERSGSESSVE QKNLARTSPG QRSRSGSSQE
1510 1520 1530 1540 1550
LDGKPSASPQ ERSESDSSPD SKPKTRTPLR QRSHSGSSPE VDSKSRHSPR
1560 1570 1580 1590 1600
LSRSGSSPEM KDKPRVLQRA QSGTDSSPEH KIPAPRALPR HSRSGSSSKE
1610 1620 1630 1640 1650
RGPSPEGSSS SESSPEHAPK SRTARRGSRS SIEPKTKSHT PPRRRSSRSS
1660 1670 1680 1690 1700
PELTRKARVS RRSRSASSSP EIRSRTPPRR RRSPSVSSPE PTEKSRSSRR
1710 1720 1730 1740 1750
RRSVSSPRTK TTSRRGRSPS PKPRGLQRSR SRSRREKTRT TRRRDRSGSS
1760 1770 1780 1790 1800
QSTSRRRQRS RSRSRVTRRR RGGSGYHSRS PTRQESSRTS SRRRRGRSRT
1810 1820 1830 1840 1850
PLTSRKRSRS RTSPAPWKRS RSRASPATHR RSRSRTPLIS RRRSRSRTSP
1860 1870 1880 1890 1900
VSRRRSRSVN RRRSRSRASP VSRRRSRSRT PPVTRRRSRS RTPTRRRSRS
1910 1920 1930 1940 1950
RTPPVTRRRS RSRTPPVTRR RSRSRTSPVT RRRSRSRTSP VTRRRSRSRT
1960 1970 1980 1990 2000
SPVTRRRSRS RTSPVTRRRS RSRTPPAIRR RSRSRTPLLP RKRSRSRSPL
2010 2020 2030 2040 2050
AIRRRSRSRT PRAARGKRSL TRSPPAIRRR SASGSSSDRS RSATPPATRN
2060 2070 2080 2090 2100
HSGSRTPPVA LSSSRMSCFS RPSMSPTPLD RCRSPGMLEP LGSARTPMSV
2110 2120 2130 2140 2150
LQQTGGSMMD GPGPRIPDHP RSSVPENHAQ SRIALALTAI SLGTARPPPS
2160 2170 2180 2190 2200
MSAAGLAARM SQVPAPVPLM SLRTAPAANL ASRIPAASAA AMNLASARTS
2210 2220 2230 2240 2250
AIPASVNLAD SRTPAAAAAM NLASPRTAVA PSAVNLADPR TPAASAVNLA
2260 2270 2280 2290 2300
GARTPAALAA LSLTGSGTPP TAANYPSSSR TPQAPTPANL VVGPRSAHGT
2310 2320 2330 2340 2350
APVNIAGSRT PAGLAPTNLS SSRMAPALSG ANLTSPRVPL SAYDRVSGRT
2360 2370 2380 2390 2400
SPLMLDRARS RTPPSAPSQS RMTSERERAP SPASRMVQAS SQSLLPPAQD
2410 2420 2430 2440 2450
RPRSPVPSAF SDQSRSVVQT TPVAGSQSLS SGTVAKSTSS ASDHNGMLSG
2460 2470 2480 2490 2500
PAPGISHAEG GEPPASTGAQ QPSTLAALQP AKERRSSSSS SSSSSSSSSS
2510 2520 2530 2540 2550
SSSSSSSSSS GSSSSDSEGS SLPAQPEVAL KRVPSPTPVP KEAIREGRPQ
2560 2570 2580 2590 2600
EPTPAKRKRR SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS
2610 2620 2630 2640 2650
SSPSPAKPGP QALPKPASPK KPPPGERRSR SPRKPIDSLR DSRSLSYSPV
2660 2670 2680 2690 2700
ERRQPSPQPS PRDLQSSERV SWRGQRGDSH SPGHKRKETP SPRSNRHRSS

RSP
Length:2,703
Mass (Da):294,840
Last modified:July 27, 2011 - v3
Checksum:iF144CB3EB1E8DF5B
GO
Isoform 2 (identifier: Q8BTI8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: Missing.

Show »
Length:2,607
Mass (Da):283,578
Checksum:iFBC77BF091726AA3
GO
Isoform 3 (identifier: Q8BTI8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2486-2585: Missing.

Show »
Length:2,603
Mass (Da):285,154
Checksum:iA1D8F0A13CFD5BE3
GO

Sequence cautioni

The sequence AAH27781.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti373 – 3731V → D in BAC41104 (PubMed:16141072).Curated
Sequence conflicti373 – 3731V → D in BAE42172 (PubMed:16141072).Curated
Sequence conflicti428 – 4281G → V in BAC41104 (PubMed:16141072).Curated
Sequence conflicti428 – 4281G → V in BAE42172 (PubMed:16141072).Curated
Sequence conflicti618 – 6181A → T in BAC41104 (PubMed:16141072).Curated
Sequence conflicti618 – 6181A → T in BAE42172 (PubMed:16141072).Curated
Sequence conflicti927 – 9271I → V in BAC41104 (PubMed:16141072).Curated
Sequence conflicti967 – 9671L → P in BAC41104 (PubMed:16141072).Curated
Sequence conflicti967 – 9671L → P in BAC65530 (PubMed:12693553).Curated
Sequence conflicti1255 – 12551E → G in BAC41104 (PubMed:16141072).Curated
Sequence conflicti1639 – 16391H → R in BAC41104 (PubMed:16141072).Curated
Sequence conflicti1639 – 16391H → R in BAC65530 (PubMed:12693553).Curated
Sequence conflicti1835 – 18351R → I in BAC41104 (PubMed:16141072).Curated
Sequence conflicti2418 – 24181V → A in BAC41104 (PubMed:16141072).Curated
Sequence conflicti2418 – 24181V → A in AAH27781 (PubMed:15489334).Curated
Sequence conflicti2418 – 24181V → A in BAC65530 (PubMed:12693553).Curated
Sequence conflicti2628 – 26281R → G in BAC41104 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9696Missing in isoform 2. 1 PublicationVSP_020188Add
BLAST
Alternative sequencei2486 – 2585100Missing in isoform 3. 1 PublicationVSP_020189Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK090123 mRNA. Translation: BAC41104.1.
AK171001 mRNA. Translation: BAE42172.1.
AC122821 Genomic DNA. No translation available.
BC027781 mRNA. Translation: AAH27781.1. Different initiation.
BC092355 mRNA. Translation: AAH92355.1.
AK122248 mRNA. Translation: BAC65530.1.
CCDSiCCDS37475.1. [Q8BTI8-2]
RefSeqiNP_780438.2. NM_175229.3. [Q8BTI8-2]
XP_006525139.1. XM_006525076.2. [Q8BTI8-1]
XP_006525140.1. XM_006525077.2. [Q8BTI8-1]
UniGeneiMm.436876.
Mm.5222.

Genome annotation databases

EnsembliENSMUST00000088621; ENSMUSP00000085993; ENSMUSG00000039218. [Q8BTI8-2]
ENSMUST00000190686; ENSMUSP00000139842; ENSMUSG00000039218. [Q8BTI8-1]
GeneIDi75956.
KEGGimmu:75956.
UCSCiuc008atn.1. mouse. [Q8BTI8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK090123 mRNA. Translation: BAC41104.1.
AK171001 mRNA. Translation: BAE42172.1.
AC122821 Genomic DNA. No translation available.
BC027781 mRNA. Translation: AAH27781.1. Different initiation.
BC092355 mRNA. Translation: AAH92355.1.
AK122248 mRNA. Translation: BAC65530.1.
CCDSiCCDS37475.1. [Q8BTI8-2]
RefSeqiNP_780438.2. NM_175229.3. [Q8BTI8-2]
XP_006525139.1. XM_006525076.2. [Q8BTI8-1]
XP_006525140.1. XM_006525077.2. [Q8BTI8-1]
UniGeneiMm.436876.
Mm.5222.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217871. 4 interactions.
IntActiQ8BTI8. 2 interactions.
MINTiMINT-4112373.
STRINGi10090.ENSMUSP00000085993.

PTM databases

iPTMnetiQ8BTI8.
PhosphoSiteiQ8BTI8.

2D gel databases

REPRODUCTION-2DPAGEIPI00225062.
IPI00785240.

Proteomic databases

EPDiQ8BTI8.
MaxQBiQ8BTI8.
PaxDbiQ8BTI8.
PRIDEiQ8BTI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000088621; ENSMUSP00000085993; ENSMUSG00000039218. [Q8BTI8-2]
ENSMUST00000190686; ENSMUSP00000139842; ENSMUSG00000039218. [Q8BTI8-1]
GeneIDi75956.
KEGGimmu:75956.
UCSCiuc008atn.1. mouse. [Q8BTI8-1]

Organism-specific databases

CTDi23524.
MGIiMGI:1923206. Srrm2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1869. Eukaryota.
ENOG4111F3M. LUCA.
GeneTreeiENSGT00730000110977.
HOGENOMiHOG000154424.
HOVERGENiHBG093999.
InParanoidiQ8BTI8.
KOiK13172.
OMAiPEMKKSH.
OrthoDBiEOG70W3CH.
TreeFamiTF335721.

Miscellaneous databases

ChiTaRSiSrrm2. mouse.
NextBioi344335.
PROiQ8BTI8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BTI8.
CleanExiMM_SRRM2.
ExpressionAtlasiQ8BTI8. baseline and differential.
GenevisibleiQ8BTI8. MM.

Family and domain databases

InterProiIPR013170. mRNA_splic_Cwf21_dom.
IPR024945. Spt5_C_dom.
[Graphical view]
PfamiPF08312. cwf21. 1 hit.
[Graphical view]
SMARTiSM01104. CTD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-745 (ISOFORM 1).
    Strain: NOD.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] OF 1-191 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2060-2703 (ISOFORM 3).
    Strain: FVB/N and NMRI.
    Tissue: Mammary tumor.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 944-968; 1338-1349 AND 1924-1932, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 950-2703 (ISOFORMS 1/2).
    Tissue: Brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1343, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  7. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-349; SER-351; SER-402; SER-406; SER-433; SER-434; SER-435; THR-841; THR-955; SER-1048; SER-1068; SER-1077; SER-1216; SER-1269; SER-1305; SER-1338; SER-1339; SER-1343; SER-1380; SER-1576; SER-1577; SER-2052; SER-2054; THR-2056; SER-2073; SER-2075; SER-2224 AND SER-2404, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-351; SER-433; SER-434; SER-435; SER-773; SER-775; SER-778; SER-1216; SER-1305; SER-2052; SER-2054 AND THR-2056, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433; SER-434; SER-435; THR-973; SER-1305; SER-1338; SER-1339; SER-1343; SER-1360; SER-1400; SER-1465; THR-1467; SER-2224; SER-2335; SER-2381 AND SER-2404, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433; SER-434; SER-435; SER-531; SER-533; SER-1151; SER-1338; SER-1339; SER-1343; SER-1360; SER-1572; SER-1576; SER-1577; SER-1982; SER-1984; THR-1986; SER-2052; SER-2054; THR-2056; SER-2224; SER-2335; SER-2351; SER-2404; SER-2646; SER-2648; SER-2656 AND SER-2660, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-310; SER-323; SER-349; SER-351; SER-402; SER-406; SER-422; SER-433; SER-434; SER-435; SER-438; SER-773; SER-778; SER-829; THR-831; THR-841; SER-882; SER-946; SER-949; THR-955; THR-973; SER-984; SER-993; THR-995; SER-1011; SER-1038; THR-1044; SER-1048; SER-1067; SER-1068; THR-1071; SER-1077; SER-1097; SER-1216; SER-1225; SER-1229; SER-1230; SER-1269; SER-1305; SER-1338; SER-1339; SER-1340; SER-1343; SER-1360; SER-1380; SER-1400; THR-1428; SER-1508; SER-1572; SER-1576; SER-1577; SER-1813; SER-2052; SER-2054; THR-2056; SER-2070; SER-2073; SER-2075; SER-2084; SER-2224; SER-2335; SER-2351; SER-2404; SER-2535 AND SER-2656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSRRM2_MOUSE
AccessioniPrimary (citable) accession number: Q8BTI8
Secondary accession number(s): E9QNB0
, Q3TBY5, Q569P9, Q80U37, Q8K383
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: July 27, 2011
Last modified: March 16, 2016
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.