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Reviewed, UniProtKB/Swiss-Prot Q9UQ35 (SRRM2_HUMAN)

Last modified May 5, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Serine/arginine repetitive matrix protein 2
Alternative name(s):
    Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa
      Short name=Ser/Arg-related nuclear matrix protein
      Short name=SR-related nuclear matrix protein of 300 kDa
    Splicing coactivator subunit SRm300
    300 kDa nuclear matrix antigen
Gene names
Name: SRRM2
Synonyms: KIAA0324, SRL300, SRM300
ORF Names: HSPC075
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length2752 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Part of pre- and post-splicing multiprotein mRNP complexes. May be involved in pre-mRNA processing events. 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, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.

Subcellular location

Nucleus speckle.

Tissue specificity

Expressed in liver, placenta, and white blood cells. Ref.1

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.1 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

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: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

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Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

spliceosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 27522752Serine/arginine repetitive matrix protein 2
PRO_0000248154

Regions

Region197 – 25963Sufficient for RNA-binding
Coiled coil60 – 9233 Potential
Compositional bias177 – 27312555Ser-rich
Compositional bias186 – 24661Lys-rich
Compositional bias350 – 44798Pro-rich
Compositional bias462 – 816355Arg-rich
Compositional bias1666 – 2089424Arg-rich
Compositional bias2182 – 2378197Ala-rich
Compositional bias2673 – 275078Arg-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7
Modified residue1421Phosphoserine Ref.11
Modified residue2501Phosphoserine Ref.11
Modified residue2521Phosphothreonine Ref.11
Modified residue2741Phosphothreonine Ref.11
Modified residue2951Phosphoserine Ref.12 Ref.17 Ref.19 Ref.20
Modified residue2971Phosphoserine Ref.11 Ref.12 Ref.17 Ref.19 Ref.20
Modified residue3221Phosphoserine Ref.20
Modified residue3231Phosphoserine Ref.17 Ref.20
Modified residue3511Phosphoserine Ref.11
Modified residue3531Phosphoserine Ref.11
Modified residue3671Phosphothreonine Ref.11 Ref.14
Modified residue3771Phosphoserine Ref.17 Ref.18
Modified residue3831Phosphothreonine Ref.17
Modified residue3841Phosphothreonine Ref.17
Modified residue3871Phosphoserine Ref.17 Ref.18
Modified residue3951Phosphoserine Ref.17
Modified residue3981Phosphoserine Ref.17 Ref.18
Modified residue4001Phosphothreonine Ref.17
Modified residue4041Phosphoserine By similarity
Modified residue4081Phosphoserine By similarity
Modified residue4151Phosphoserine Ref.17
Modified residue4181Phosphoserine Ref.17
Modified residue4241Phosphoserine Ref.11
Modified residue4281Phosphothreonine Ref.17
Modified residue4351Phosphoserine Ref.17
Modified residue4361Phosphoserine By similarity
Modified residue4371Phosphoserine By similarity
Modified residue4401Phosphoserine Ref.17
Modified residue5341Phosphoserine By similarity
Modified residue5361Phosphoserine By similarity
Modified residue7551Phosphoserine Ref.17
Modified residue7591Phosphoserine Ref.17
Modified residue7611Phosphoserine Ref.17
Modified residue7631Phosphoserine Ref.17
Modified residue7641Phosphoserine Ref.17
Modified residue7741Phosphoserine Ref.17
Modified residue7781Phosphoserine Ref.14 Ref.17
Modified residue7801Phosphoserine Ref.14 Ref.17
Modified residue7831Phosphoserine Ref.14 Ref.17
Modified residue8201Phosphoserine Ref.11
Modified residue8461Phosphoserine By similarity
Modified residue8481Phosphothreonine By similarity
Modified residue8571Phosphoserine Ref.11
Modified residue8661Phosphothreonine Ref.11
Modified residue8711Phosphoserine Ref.14
Modified residue8751Phosphoserine Ref.19
Modified residue8761Phosphoserine Ref.14
Modified residue8831Phosphoserine Ref.17
Modified residue8851Phosphothreonine Ref.17
Modified residue8901Phosphoserine Ref.17
Modified residue8941Phosphoserine Ref.17
Modified residue8951Phosphoserine Ref.17
Modified residue9011Phosphoserine Ref.11
Modified residue9031Phosphothreonine Ref.11
Modified residue9081Phosphoserine Ref.11
Modified residue9141Phosphoserine Ref.11
Modified residue9241Phosphoserine Ref.12
Modified residue9501Phosphoserine Ref.17
Modified residue9521Phosphoserine Ref.14 Ref.17
Modified residue9541Phosphoserine Ref.14 Ref.17 Ref.19
Modified residue9721Phosphoserine By similarity
Modified residue9731Phosphoserine By similarity
Modified residue9741Phosphoserine By similarity
Modified residue9831Phosphothreonine Ref.17 Ref.19
Modified residue9881Phosphoserine Ref.11 Ref.17 Ref.19
Modified residue9941Phosphoserine Ref.11 Ref.17
Modified residue9961Phosphotyrosine Ref.17
Modified residue10031Phosphothreonine Ref.11 Ref.19
Modified residue10141Phosphoserine Ref.19
Modified residue10431Phosphothreonine Ref.11 Ref.19
Modified residue10631Phosphothreonine Ref.17
Modified residue10691Phosphoserine Ref.11 Ref.17
Modified residue10711Phosphothreonine Ref.17
Modified residue10721Phosphoserine Ref.14 Ref.17
Modified residue10731Phosphoserine Ref.11 Ref.14 Ref.17
Modified residue10791Phosphoserine Ref.11
Modified residue10831Phosphoserine Ref.11
Modified residue10991Phosphoserine Ref.17
Modified residue11011Phosphoserine Ref.17
Modified residue11031Phosphoserine Ref.11 Ref.17
Modified residue11061Phosphothreonine Ref.17 Ref.19
Modified residue11101Phosphoserine Ref.17
Modified residue11121Phosphoserine Ref.17 Ref.19
Modified residue11241Phosphoserine Ref.11 Ref.15 Ref.17
Modified residue11291Phosphoserine Ref.17
Modified residue11321Phosphoserine Ref.11
Modified residue11791Phosphoserine Ref.11
Modified residue11881Phosphoserine Ref.15
Modified residue12051Phosphothreonine Ref.17
Modified residue12081Phosphothreonine Ref.17
Modified residue12141Phosphoserine Ref.11
Modified residue12181Phosphoserine Ref.17
Modified residue12191Phosphoserine Ref.11 Ref.17
Modified residue12571Phosphoserine By similarity
Modified residue13201Phosphoserine Ref.11 Ref.17 Ref.19
Modified residue13261Phosphoserine Ref.11
Modified residue13291Phosphoserine Ref.15 Ref.17
Modified residue13481Phosphoserine By similarity
Modified residue13781Phosphoserine By similarity
Modified residue13821Phosphoserine Ref.12
Modified residue13831Phosphoserine By similarity
Modified residue13841Phosphoserine By similarity
Modified residue13871Phosphoserine Ref.12
Modified residue13971Phosphoserine Ref.11 Ref.17
Modified residue13981Phosphoserine Ref.17
Modified residue14031Phosphoserine Ref.17
Modified residue14041Phosphoserine Ref.11 Ref.17 Ref.20
Modified residue14131Phosphothreonine Ref.17 Ref.20
Modified residue14151Phosphoserine Ref.17
Modified residue14191Phosphoserine Ref.19
Modified residue14201Phosphoserine By similarity
Modified residue14211Phosphoserine Ref.11
Modified residue14231Phosphoserine Ref.11
Modified residue14241Phosphoserine By similarity
Modified residue14411Phosphoserine Ref.11
Modified residue14431Phosphoserine Ref.11
Modified residue14441Phosphoserine Ref.11
Modified residue14531Phosphothreonine Ref.11
Modified residue14581Phosphoserine By similarity
Modified residue14831Phosphoserine Ref.11
Modified residue14921Phosphothreonine Ref.17
Modified residue14971Phosphoserine Ref.12 Ref.17
Modified residue14991Phosphoserine Ref.11 Ref.17
Modified residue15011Phosphoserine Ref.11 Ref.12 Ref.17
Modified residue15021Phosphoserine Ref.11 Ref.12 Ref.17
Modified residue15111Phosphothreonine Ref.11
Modified residue15171Phosphoserine Ref.11
Modified residue15191Phosphoserine Ref.11
Modified residue15221Phosphoserine Ref.11
Modified residue15311Phosphothreonine Ref.16
Modified residue15591Phosphoserine Ref.11
Modified residue15711Phosphothreonine Ref.17
Modified residue15791Phosphoserine Ref.11 Ref.17
Modified residue15811Phosphoserine Ref.11 Ref.17
Modified residue15821Phosphoserine Ref.11 Ref.17
Modified residue15921Phosphoserine Ref.17
Modified residue15961Phosphoserine Ref.17
Modified residue15981Phosphoserine Ref.17
Modified residue16001Phosphoserine Ref.11 Ref.12 Ref.17
Modified residue16011Phosphoserine Ref.11 Ref.12 Ref.17
Modified residue16161Phosphoserine Ref.12 Ref.17
Modified residue16181Phosphoserine Ref.11 Ref.17
Modified residue16201Phosphoserine Ref.12 Ref.17
Modified residue16211Phosphoserine Ref.11 Ref.12 Ref.17
Modified residue16361Phosphoserine Ref.17
Modified residue16381Phosphoserine Ref.17
Modified residue16401Phosphoserine Ref.17
Modified residue16411Phosphoserine Ref.17
Modified residue16571Phosphoserine Ref.17
Modified residue16581Phosphoserine Ref.17
Modified residue16821Phosphoserine Ref.17
Modified residue16841Phosphothreonine Ref.17
Modified residue16901Phosphoserine Ref.17
Modified residue16911Phosphoserine Ref.17
Modified residue16931Phosphoserine Ref.17
Modified residue16941Phosphoserine Ref.17
Modified residue18421Phosphoserine By similarity
Modified residue18441Phosphothreonine By similarity
Modified residue18761Phosphoserine Ref.17
Modified residue18781Phosphoserine Ref.14 Ref.17 Ref.19
Modified residue18801Phosphothreonine Ref.11 Ref.14 Ref.17 Ref.19
Modified residue19581Phosphoserine Ref.17
Modified residue19601Phosphoserine Ref.17
Modified residue19621Phosphothreonine Ref.11 Ref.17
Modified residue19751Phosphoserine Ref.16
Modified residue20111Phosphoserine By similarity
Modified residue20181Phosphoserine Ref.17
Modified residue20201Phosphoserine Ref.17
Modified residue20221Phosphothreonine Ref.17
Modified residue20301Phosphoserine Ref.17
Modified residue20321Phosphoserine Ref.14 Ref.15 Ref.17
Modified residue20341Phosphothreonine Ref.14 Ref.17
Modified residue20421Phosphoserine Ref.17
Modified residue20441Phosphoserine Ref.11 Ref.14 Ref.15 Ref.17
Modified residue20461Phosphoserine Ref.11 Ref.14 Ref.17 Ref.19
Modified residue20671Phosphoserine Ref.15 Ref.17
Modified residue20691Phosphothreonine Ref.17
Modified residue20711Phosphoserine Ref.11 Ref.17
Modified residue20921Phosphothreonine Ref.11
Modified residue21001Phosphoserine Ref.12 Ref.19
Modified residue21021Phosphoserine By similarity
Modified residue21041Phosphothreonine Ref.11
Modified residue21211Phosphoserine By similarity
Modified residue21321Phosphoserine Ref.19
Modified residue22721Phosphoserine Ref.11 Ref.14 Ref.15 Ref.17 Ref.20
Modified residue22891Phosphothreonine Ref.14
Modified residue22911Phosphothreonine Ref.14
Modified residue23161Phosphothreonine Ref.14
Modified residue23351Phosphoserine Ref.11
Modified residue23821Phosphoserine Ref.11 Ref.14
Modified residue23971Phosphothreonine Ref.19
Modified residue23981Phosphoserine Ref.11 Ref.19 Ref.20
Modified residue24071Phosphoserine Ref.11 Ref.17 Ref.20
Modified residue24091Phosphothreonine Ref.11 Ref.17 Ref.20
Modified residue24261Phosphoserine Ref.11
Modified residue24361Phosphoserine Ref.18
Modified residue24491Phosphoserine Ref.11 Ref.14
Modified residue24531Phosphoserine Ref.18
Modified residue25811Phosphoserine Ref.11 Ref.19
Modified residue25831Phosphothreonine By similarity
Modified residue26751Phosphoserine Ref.13 Ref.21
Modified residue26771Phosphoserine Ref.13 Ref.21
Modified residue26841Phosphoserine Ref.13
Modified residue26881Phosphoserine Ref.13 Ref.20
Modified residue26901Phosphoserine Ref.21
Modified residue26921Phosphoserine Ref.11 Ref.14 Ref.15 Ref.21
Modified residue26931Phosphotyrosine By similarity
Modified residue26941Phosphoserine Ref.11 Ref.14 Ref.15 Ref.19 Ref.20 Ref.21
Modified residue27021Phosphoserine Ref.13
Modified residue27061Phosphoserine Ref.13
Modified residue27141Phosphoserine Ref.11
Modified residue27381Phosphothreonine Ref.13
Modified residue27401Phosphoserine Ref.13

Natural variations

Alternative sequence1 – 9696Missing in isoform 3.
VSP_020184
Alternative sequence394 – 40714PSEAS…RSPPK → SPQLFMFLKGILVF in isoform 3.
VSP_020185
Alternative sequence408 – 27522345Missing in isoform 3.
VSP_020186
Alternative sequence2023 – 2440418Missing in isoform 2.
VSP_020187
Natural variant8041P → T: dbSNP rs2240140. Ref.3
VAR_027259
Natural variant8561T → R: dbSNP rs12185191.
VAR_048868
Natural variant8831S → C: dbSNP rs17136053.
VAR_027260

Experimental info

Sequence conflict1571A → V in AAF28898. Ref.8
Sequence conflict178 – 1792SS → NN in AAF21439. Ref.2
Sequence conflict1951D → K in AAH07752. Ref.6
Sequence conflict3141G → S in AAF21439. Ref.2
Sequence conflict3211P → A in AAF21439. Ref.2
Sequence conflict14741S → F in BAA83716. Ref.1
Sequence conflict14741S → F in BAA83718. Ref.1

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Sequences

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

Last modified March 6, 2007. Version 2.
Checksum: 7A5DCEB9B50AA912

FASTA2,752299,615
        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

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Isoform 2.

Checksum: 22CE5B02DA3E03CC
Show »

FASTA2,334256,645
Isoform 3.

Checksum: F8391BC3C125F65B
Show »

FASTA31134,212

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References

« Hide 'large scale' references
[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: 11004489] [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: 10668804] [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: 9205841] [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. expand/collapse author list , 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: 15616553] [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. expand/collapse author list , 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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1018 AND 2555-2752.
Tissue: Blood, Embryonic testis carcinoma, Placenta, Retinoblastoma and Rhabdomyosarcoma.
[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: 9531537] [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: 11991638] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
[11]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-250; THR-252; THR-274; SER-297; SER-351; SER-353; THR-367; SER-424; SER-820; SER-857; THR-866; SER-901; THR-903; SER-908; SER-914; SER-988; SER-994; THR-1003; THR-1043; SER-1069; SER-1073; SER-1079; SER-1083; SER-1103; SER-1124; SER-1132; SER-1179; SER-1214; SER-1219; SER-1320; SER-1326; SER-1397; SER-1404; SER-1421; SER-1423; SER-1441; SER-1443; SER-1444; THR-1453; SER-1483; SER-1499; SER-1501; SER-1502; THR-1511; SER-1517; SER-1519; SER-1522; SER-1559; SER-1579; SER-1581; SER-1582; SER-1600; SER-1601; SER-1618; SER-1621; THR-1880; THR-1962; SER-2044; SER-2046; SER-2071; THR-2092; THR-2104; SER-2272; SER-2335; SER-2382; SER-2398; SER-2407; THR-2409; SER-2426; SER-2449; SER-2581; SER-2692; SER-2694 AND SER-2714, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-924; SER-1382; SER-1387; SER-1497; SER-1501; SER-1502; SER-1600; SER-1601; SER-1616; SER-1620; SER-1621 AND SER-2100, MASS SPECTROMETRY.
[13]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2675; SER-2677; SER-2684; SER-2688; SER-2702; SER-2706; THR-2738 AND SER-2740, MASS SPECTROMETRY.
Tissue: Epithelium.
[14]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-367; SER-778; SER-780; SER-783; SER-871; SER-876; SER-952; SER-954; SER-1072; SER-1073; SER-1878; THR-1880; SER-2032; THR-2034; SER-2044; SER-2046; SER-2272; THR-2289; THR-2291; THR-2316; SER-2382; SER-2449; SER-2692 AND SER-2694, MASS SPECTROMETRY.
Tissue: Epithelium.
[15]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1124; SER-1188; SER-1329; SER-2032; SER-2044; SER-2067; SER-2272; SER-2692 AND SER-2694, MASS SPECTROMETRY.
Tissue: Epithelium.
[16]"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: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1531 AND SER-1975, MASS SPECTROMETRY.
Tissue: Epithelium.
[17]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-323; SER-377; THR-383; THR-384; SER-387; SER-395; SER-398; THR-400; SER-415; SER-418; THR-428; SER-435; SER-440; SER-755; SER-759; SER-761; SER-763; SER-764; SER-774; SER-778; SER-780; SER-783; SER-883; THR-885; SER-890; SER-894; SER-895; SER-950; SER-952; SER-954; THR-983; SER-988; SER-994; TYR-996; THR-1063; SER-1069; THR-1071; SER-1072; SER-1073; SER-1099; SER-1101; SER-1103; THR-1106; SER-1110; SER-1112; SER-1124; SER-1129; THR-1205; THR-1208; SER-1218; SER-1219; SER-1320; SER-1329; SER-1397; SER-1398; SER-1403; SER-1404; THR-1413; SER-1415; THR-1492; SER-1497; SER-1499; SER-1501; SER-1502; THR-1571; SER-1579; SER-1581; SER-1582; SER-1592; SER-1596; SER-1598; SER-1600; SER-1601; SER-1616; SER-1618; SER-1620; SER-1621; SER-1636; SER-1638; SER-1640; SER-1641; SER-1657; SER-1658; SER-1682; THR-1684; SER-1690; SER-1691; SER-1693; SER-1694; SER-1876; SER-1878; THR-1880; SER-1958; SER-1960; THR-1962; SER-2018; SER-2020; THR-2022; SER-2030; SER-2032; THR-2034; SER-2042; SER-2044; SER-2046; SER-2067; THR-2069; SER-2071; SER-2272; SER-2407 AND THR-2409, MASS SPECTROMETRY.
[18]"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: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-387; SER-398; SER-2436 AND SER-2453, MASS SPECTROMETRY.
[19]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-875; SER-954; THR-983; SER-988; THR-1003; SER-1014; THR-1043; THR-1106; SER-1112; SER-1320; SER-1419; SER-1878; THR-1880; SER-2046; SER-2100; SER-2132; THR-2397; SER-2398; SER-2581 AND SER-2694, MASS SPECTROMETRY.
[20]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-322; SER-323; SER-1404; THR-1413; SER-2272; SER-2398; SER-2407; THR-2409; SER-2688 AND SER-2694, MASS SPECTROMETRY.
[21]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2675; SER-2677; SER-2690; SER-2692 AND SER-2694, MASS SPECTROMETRY.
[22]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

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Cross-references

Sequence databases

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.
BC007752 mRNA. Translation: AAH07752.1.
BC009062 mRNA. Translation: AAH09062.1.
BC032416 mRNA. Translation: AAH32416.1.
BC041155 mRNA. Translation: AAH41155.1.
BC070050 mRNA. Translation: AAH70050.1. Sequence problems.
AF161338 mRNA. Translation: AAF28898.1. Frameshift.
IPIIPI00782992.
IPI00784560.
IPI00785023.
RefSeqNP_057417.3.
UniGeneHs.712559

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9UQ35. 10 interactions.

PTM databases

PhosphoSiteQ9UQ35.

Proteomic databases

PRIDEQ9UQ35.

Genome annotation databases

EnsemblENSG00000167978. Homo sapiens. [Contig view]
GeneID23524.
KEGGhsa:23524.
NMPDRfig|9606.3.peg.11582.

Organism-specific databases

GeneCardsGC16P002742.
HGNCHGNC:16639. SRRM2.
MIM606032. gene.
PharmGKBPA38178.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9UQ35.
OMAQ9UQ35. TSPAPWK.

Gene expression databases

ArrayExpressQ9UQ35.
BgeeQ9UQ35.
GermOnlineENSG00000167978. Homo sapiens.

Family and domain databases

InterProIPR013170. mRNA_splic_Cwf21.
[Graphical view]
PfamPF08312. cwf21. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio45984.
SOURCESearch...

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Entry information

Entry nameSRRM2_HUMAN
AccessionPrimary (citable) accession number: Q9UQ35
Secondary accession number(s): A6NKB9 expand/collapse secondary AC list , 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: May 5, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents