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Q9UQ35 (SRRM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length2752 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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 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 Ref.25
Modified residue241Phosphoserine
Modified residue1451Phosphotyrosine Ref.20
Modified residue1691N6-acetyllysine Ref.21
Modified residue2201Phosphoserine Ref.22
Modified residue2221Phosphoserine Ref.22
Modified residue2861Phosphothreonine Ref.22
Modified residue2951Phosphoserine Ref.17 Ref.22
Modified residue2971Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue3001Phosphoserine Ref.22
Modified residue3221Phosphoserine Ref.17 Ref.20
Modified residue3231Phosphoserine Ref.17 Ref.20
Modified residue3331Phosphoserine Ref.24
Modified residue3511Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
Modified residue3531Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
Modified residue3571Phosphoserine Ref.20
Modified residue3581Phosphoserine Ref.20
Modified residue3591Phosphothreonine Ref.20
Modified residue3671Phosphothreonine Ref.13 Ref.20 Ref.22
Modified residue3771Phosphoserine Ref.13 Ref.15 Ref.17 Ref.20 Ref.22 Ref.24
Modified residue3871Phosphoserine Ref.17
Modified residue3981Phosphoserine Ref.17 Ref.24
Modified residue4041Phosphoserine Ref.24
Modified residue4081Phosphoserine Ref.24
Modified residue4241Phosphoserine Ref.22 Ref.24
Modified residue4351Phosphoserine Ref.17
Modified residue4361Phosphoserine By similarity
Modified residue4371Phosphoserine By similarity
Modified residue4401Phosphoserine Ref.12 Ref.17 Ref.22 Ref.24
Modified residue4541Phosphoserine Ref.22
Modified residue4841Phosphoserine Ref.22
Modified residue4861Phosphoserine Ref.22
Modified residue5341Phosphoserine By similarity
Modified residue5361Phosphoserine By similarity
Modified residue7781Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue7801Phosphoserine Ref.17
Modified residue7831Phosphoserine Ref.17 Ref.24
Modified residue8461Phosphoserine Ref.20
Modified residue8571Phosphoserine Ref.17 Ref.20
Modified residue8641Phosphoserine Ref.17
Modified residue8661Phosphothreonine Ref.17 Ref.20 Ref.22
Modified residue8711Phosphoserine Ref.13 Ref.22
Modified residue8751Phosphoserine Ref.22
Modified residue8761Phosphoserine Ref.13 Ref.20 Ref.22 Ref.24
Modified residue9081Phosphoserine Ref.24
Modified residue9241Phosphoserine
Modified residue9501Phosphoserine Ref.17 Ref.22
Modified residue9521Phosphoserine Ref.17 Ref.20
Modified residue9541Phosphoserine Ref.13 Ref.17 Ref.20
Modified residue9571Phosphoserine Ref.17
Modified residue9681Phosphoserine Ref.17
Modified residue9701Phosphoserine Ref.17
Modified residue9721Phosphoserine Ref.17
Modified residue9731Phosphoserine Ref.22 Ref.24
Modified residue9741Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue9771Phosphothreonine Ref.24
Modified residue9831Phosphothreonine Ref.17 Ref.22
Modified residue9921Phosphoserine Ref.24
Modified residue9941Phosphoserine Ref.17 Ref.22
Modified residue10031Phosphothreonine Ref.12 Ref.17 Ref.20 Ref.22 Ref.24
Modified residue10141Phosphoserine Ref.17 Ref.22
Modified residue10281Phosphoserine Ref.17 Ref.22
Modified residue10321Phosphoserine Ref.17
Modified residue10431Phosphothreonine Ref.24
Modified residue10641Phosphoserine Ref.17
Modified residue10691Phosphoserine Ref.17 Ref.24
Modified residue10721Phosphoserine Ref.13 Ref.17
Modified residue10731Phosphoserine Ref.13 Ref.17
Modified residue10831Phosphoserine Ref.22 Ref.24
Modified residue10991Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
Modified residue11011Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
Modified residue11021Phosphoserine Ref.13 Ref.17 Ref.20
Modified residue11031Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
Modified residue11061Phosphothreonine Ref.20
Modified residue11121Phosphoserine Ref.17
Modified residue11221Phosphoserine Ref.22
Modified residue11241Phosphoserine Ref.22 Ref.24
Modified residue11291Phosphoserine Ref.24
Modified residue11321Phosphoserine Ref.12 Ref.22 Ref.24
Modified residue11521Phosphoserine Ref.22
Modified residue11791Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue11881Phosphoserine Ref.12 Ref.17 Ref.22 Ref.24
Modified residue12081Phosphothreonine Ref.17
Modified residue12141Phosphoserine Ref.20
Modified residue12191Phosphoserine Ref.22 Ref.24
Modified residue12571Phosphoserine By similarity
Modified residue13111Phosphoserine By similarity
Modified residue13181Phosphoserine Ref.17 Ref.20
Modified residue13201Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
Modified residue13261Phosphoserine Ref.17 Ref.20 Ref.22
Modified residue13291Phosphoserine Ref.12 Ref.17 Ref.20 Ref.22 Ref.24
Modified residue13361Phosphoserine Ref.22
Modified residue13481Phosphoserine By similarity
Modified residue13681Phosphoserine Ref.22
Modified residue13821Phosphoserine Ref.20 Ref.24
Modified residue13831Phosphoserine By similarity
Modified residue13871Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
Modified residue14011Phosphoserine Ref.17 Ref.20
Modified residue14031Phosphoserine Ref.20
Modified residue14041Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
Modified residue14131Phosphothreonine Ref.17 Ref.22 Ref.24
Modified residue14151Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue14211Phosphoserine Ref.22
Modified residue14231Phosphoserine By similarity
Modified residue14241Phosphoserine Ref.24
Modified residue14341Phosphothreonine Ref.22
Modified residue14441Phosphoserine Ref.17 Ref.24
Modified residue14511Phosphoserine Ref.17
Modified residue14531Phosphothreonine Ref.17
Modified residue14581Phosphoserine Ref.24
Modified residue14601Phosphoserine Ref.22
Modified residue14621Phosphoserine Ref.22
Modified residue14631Phosphoserine Ref.22 Ref.24
Modified residue14721Phosphothreonine Ref.17
Modified residue14821Phosphoserine Ref.22
Modified residue14831Phosphoserine Ref.22
Modified residue14921Phosphothreonine Ref.12 Ref.22
Modified residue14971Phosphoserine Ref.22 Ref.24
Modified residue14991Phosphoserine Ref.22 Ref.24
Modified residue15011Phosphoserine Ref.22
Modified residue15021Phosphoserine Ref.22 Ref.24
Modified residue15111Phosphothreonine Ref.17
Modified residue15171Phosphoserine Ref.24
Modified residue15191Phosphoserine Ref.24
Modified residue15211Phosphoserine Ref.24
Modified residue15221Phosphoserine Ref.17 Ref.24
Modified residue15311Phosphothreonine Ref.14 Ref.17
Modified residue15371Phosphoserine Ref.17
Modified residue15391Phosphoserine Ref.17
Modified residue15411Phosphoserine Ref.17
Modified residue15421Phosphoserine Ref.17 Ref.24
Modified residue15521Phosphoserine Ref.17 Ref.24
Modified residue15771Phosphoserine Ref.24
Modified residue15791Phosphoserine Ref.24
Modified residue15811Phosphoserine Ref.24
Modified residue15821Phosphoserine Ref.24
Modified residue15981Phosphoserine Ref.24
Modified residue16001Phosphoserine Ref.24
Modified residue16011Phosphoserine Ref.24
Modified residue16161Phosphoserine By similarity
Modified residue16201Phosphoserine By similarity
Modified residue16211Phosphoserine Ref.22
Modified residue16481Phosphoserine Ref.24
Modified residue16581Phosphoserine Ref.24
Modified residue16911Phosphoserine Ref.17
Modified residue16931Phosphoserine Ref.17
Modified residue16941Phosphoserine Ref.17 Ref.24
Modified residue16981Phosphothreonine Ref.17
Modified residue17271Phosphoserine Ref.24
Modified residue17291Phosphoserine Ref.24
Modified residue17311Phosphoserine Ref.24
Modified residue17321Phosphoserine Ref.24
Modified residue17621Phosphoserine Ref.22 Ref.24
Modified residue17641Phosphoserine Ref.22 Ref.24
Modified residue18181Phosphoserine Ref.24
Modified residue18221Phosphoserine Ref.24
Modified residue18541Phosphoserine Ref.22 Ref.24
Modified residue18571Phosphoserine Ref.22
Modified residue18761Phosphoserine Ref.17
Modified residue18781Phosphoserine Ref.17 Ref.24
Modified residue18801Phosphothreonine Ref.17
Modified residue18841Phosphoserine Ref.24
Modified residue18901Phosphoserine Ref.22 Ref.24
Modified residue18921Phosphothreonine Ref.22
Modified residue18931Phosphoserine Ref.22
Modified residue19161Phosphoserine Ref.22 Ref.24
Modified residue19191Phosphoserine Ref.22 Ref.24
Modified residue19231Phosphoserine Ref.17
Modified residue19251Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue19271Phosphothreonine Ref.17 Ref.22 Ref.24
Modified residue19311Phosphothreonine Ref.24
Modified residue19461Phosphoserine Ref.17
Modified residue19481Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue19501Phosphothreonine Ref.17 Ref.22 Ref.24
Modified residue19541Phosphothreonine Ref.24
Modified residue19581Phosphoserine Ref.17
Modified residue19601Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue19621Phosphothreonine Ref.17 Ref.22 Ref.24
Modified residue19661Phosphothreonine Ref.24
Modified residue19701Phosphoserine Ref.17 Ref.24
Modified residue19721Phosphoserine Ref.22 Ref.24
Modified residue19751Phosphoserine Ref.22 Ref.24
Modified residue19781Phosphothreonine Ref.24
Modified residue19841Phosphoserine Ref.22 Ref.24
Modified residue19871Phosphoserine Ref.22 Ref.24
Modified residue19961Phosphoserine Ref.22 Ref.24
Modified residue19991Phosphoserine Ref.22 Ref.24
Modified residue20081Phosphoserine Ref.22 Ref.24
Modified residue20111Phosphoserine Ref.22 Ref.24
Modified residue20201Phosphoserine Ref.24
Modified residue20221Phosphothreonine Ref.24
Modified residue20301Phosphoserine By similarity
Modified residue20321Phosphoserine Ref.24
Modified residue20341Phosphothreonine Ref.24
Modified residue20441Phosphoserine Ref.22 Ref.24
Modified residue20461Phosphoserine Ref.22 Ref.24
Modified residue20671Phosphoserine Ref.24
Modified residue20691Phosphothreonine Ref.22 Ref.24
Modified residue20711Phosphoserine Ref.22 Ref.24
Modified residue20901Phosphoserine Ref.24
Modified residue20921Phosphothreonine Ref.24
Modified residue21001Phosphoserine Ref.17 Ref.20
Modified residue21021Phosphoserine Ref.17 Ref.20 Ref.22
Modified residue21041Phosphothreonine Ref.17 Ref.20 Ref.22 Ref.24
Modified residue21181Phosphoserine Ref.17
Modified residue21211Phosphoserine Ref.17
Modified residue21231Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue21321Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24
Modified residue21441Phosphothreonine Ref.17
Modified residue22721Phosphoserine Ref.13 Ref.16 Ref.17 Ref.20 Ref.22 Ref.24
Modified residue22891Phosphothreonine Ref.17 Ref.20 Ref.22
Modified residue22911Phosphothreonine Ref.13
Modified residue23021Phosphothreonine Ref.17 Ref.22
Modified residue23161Phosphothreonine Ref.13 Ref.17 Ref.20
Modified residue23291Phosphothreonine Ref.17 Ref.22
Modified residue23351Phosphoserine Ref.22
Modified residue23431Phosphoserine Ref.22
Modified residue23811Phosphothreonine Ref.20
Modified residue23821Phosphoserine Ref.13 Ref.17 Ref.20 Ref.22 Ref.24
Modified residue23941Phosphoserine Ref.22
Modified residue23981Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue24071Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue24091Phosphothreonine Ref.17 Ref.22
Modified residue24121Phosphoserine Ref.17 Ref.24
Modified residue24151Phosphoserine Ref.24
Modified residue24261Phosphoserine Ref.24
Modified residue24291Phosphoserine Ref.24
Modified residue24491Phosphoserine Ref.15 Ref.17 Ref.20 Ref.22 Ref.24
Modified residue24531Phosphoserine Ref.22
Modified residue25811Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue25831Phosphothreonine Ref.22
Modified residue26641Phosphoserine Ref.22 Ref.24
Modified residue26751Phosphoserine Ref.17
Modified residue26771Phosphoserine Ref.17
Modified residue26841Phosphoserine Ref.22 Ref.24
Modified residue26881Phosphoserine Ref.22 Ref.24
Modified residue26901Phosphoserine Ref.17 Ref.22
Modified residue26921Phosphoserine Ref.17 Ref.22 Ref.24
Modified residue26941Phosphoserine Ref.13 Ref.17 Ref.22 Ref.24
Modified residue27021Phosphoserine Ref.22 Ref.24
Modified residue27061Phosphoserine Ref.22 Ref.24

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. Ref.3
Corresponds to variant rs2240140 [ dbSNP | Ensembl ].
VAR_027259
Natural variant8561T → R.
Corresponds to variant rs12185191 [ dbSNP | Ensembl ].
VAR_048868
Natural variant8831S → C.
Corresponds to variant rs17136053 [ dbSNP | Ensembl ].
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

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

« Hide

Isoform 2 [UniParc].

Checksum: 22CE5B02DA3E03CC
Show »

FASTA2,334256,645
Isoform 3 [UniParc].

Checksum: F8391BC3C125F65B
Show »

FASTA31134,212

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] [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. 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] [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. 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] [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.
RefSeqNP_057417.3. NM_016333.3.
XP_005255282.1. XM_005255225.1.
UniGeneHs.433343.

3D structure databases

ProteinModelPortalQ9UQ35.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117071. 197 interactions.
IntActQ9UQ35. 48 interactions.
MINTMINT-5006711.

PTM databases

PhosphoSiteQ9UQ35.

Polymorphism databases

DMDM143928063.

Proteomic databases

PaxDbQ9UQ35.
PRIDEQ9UQ35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301740; ENSP00000301740; ENSG00000167978.
GeneID23524.
KEGGhsa:23524.
UCSCuc002crj.1. human.

Organism-specific databases

CTD23524.
GeneCardsGC16P002769.
H-InvDBHIX0194349.
HGNCHGNC:16639. SRRM2.
HPAHPA041411.
MIM606032. gene.
neXtProtNX_Q9UQ35.
PharmGKBPA38178.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG093999.
InParanoidQ9UQ35.
KOK13172.
OMACFSRPSM.
OrthoDBEOG70W3CH.
PhylomeDBQ9UQ35.
TreeFamTF335721.

Gene expression databases

ArrayExpressQ9UQ35.
BgeeQ9UQ35.
GenevestigatorQ9UQ35.

Family and domain databases

InterProIPR013170. mRNA_splic_Cwf21.
IPR024945. Spt5_C_dom.
[Graphical view]
PfamPF08312. cwf21. 1 hit.
[Graphical view]
SMARTSM01104. CTD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSRRM2. human.
GeneWikiSRRM2.
GenomeRNAi23524.
NextBio45984.
PROQ9UQ35.
SOURCESearch...

Entry information

Entry nameSRRM2_HUMAN
AccessionPrimary (citable) accession number: Q9UQ35
Secondary accession number(s): A6NKB9 expand/collapse secondary AC list , 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: February 19, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

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

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