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Q96T58 (MINT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Msx2-interacting protein
Alternative name(s):
SMART/HDAC1-associated repressor protein
SPEN homolog
Gene names
Name:SPEN
Synonyms:KIAA0929, MINT, SHARP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3664 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May serve as a nuclear matrix platform that organizes and integrates transcriptional responses. In osteoblasts, supports transcription activation: synergizes with RUNX2 to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) By similarity. Has also been shown to be an essential corepressor protein, which probably regulates different key pathways such as the Notch pathway. Negative regulator of the Notch pathway via its interaction with RBPSUH, which prevents the association between NOTCH1 and RBPSUH, and therefore suppresses the transactivation activity of Notch signaling. Blocks the differentiation of precursor B-cells into marginal zone B-cells. Probably represses transcription via the recruitment of large complexes containing histone deacetylase proteins. May bind both to DNA and RNA. Ref.1 Ref.7

Subunit structure

Interacts with MSX2 and HIPK3 By similarity. Interacts with NCOR2, HDAC1, HDAC2, RBBP4, MBD3 and MTA1L1. Interacts with RBPSUH; this interaction may prevent the interaction between RBPSUH and NOTCH1. Interacts with the nuclear receptors RAR and PPARD. Interacts with RAR in absence of ligand. Binds to the steroid receptor RNA coactivator SRA. Interacts with Epstein-Barr virus BSFL2/BMLF1. Ref.1 Ref.6 Ref.7 Ref.8

Subcellular location

Nucleus. Note: Associates with chromatin. Ref.1

Tissue specificity

Expressed at high level in brain, testis, spleen and thymus. Expressed at intermediate level in kidney, liver, mammary gland and skin.

Induction

By 17-beta-estradiol. Ref.1

Domain

The RID domain mediates the interaction with nuclear receptors By similarity. Ref.16

The SPOC domain, which mediates the interaction with NCOR2, is essential for the repressive activity. Ref.16

Sequence similarities

Belongs to the RRM Spen family.

Contains 1 RID (receptor interacting) domain.

Contains 4 RRM (RNA recognition motif) domains.

Contains 1 SPOC domain.

Sequence caution

The sequence BAA91405.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB14324.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB51072.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processHost-virus interaction
Notch signaling pathway
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
   LigandDNA-binding
RNA-binding
   Molecular functionActivator
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16287852. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of neurogenesis

Inferred from mutant phenotype PubMed 16287852. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleus

Inferred from direct assay. Source: HPA

transcriptional repressor complex

Inferred from direct assay PubMed 16287852. Source: BHF-UCL

   Molecular_functionRNA polymerase II transcription factor binding

Inferred from physical interaction PubMed 16287852. Source: BHF-UCL

RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 16287852. Source: BHF-UCL

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

single-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

transcription corepressor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163333EBI-765739,EBI-389883

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 36643664Msx2-interacting protein
PRO_0000081627

Regions

Domain6 – 8176RRM 1
Domain335 – 41581RRM 2
Domain438 – 51376RRM 3
Domain517 – 58973RRM 4
Domain2201 – 2707507RID
Domain3498 – 3664167SPOC
DNA binding1 – 573573 By similarity
Region2130 – 2464335Interaction with MSX2 By similarity
Region2709 – 2870162Interaction with RBPSUH By similarity
Coiled coil688 – 71528 Potential
Coiled coil977 – 100428 Potential
Coiled coil1170 – 119122 Potential
Coiled coil1408 – 142821 Potential
Coiled coil1496 – 152934 Potential
Coiled coil1592 – 161221 Potential
Coiled coil1928 – 194417 Potential
Compositional bias125 – 277153Arg-rich
Compositional bias240 – 32586Ser-rich
Compositional bias616 – 810195Arg-rich
Compositional bias624 – 69774Tyr-rich
Compositional bias2428 – 252093Pro-rich
Compositional bias3220 – 3482263Pro-rich

Amino acid modifications

Modified residue3091Phosphoserine Ref.14
Modified residue6231Phosphoserine Ref.14
Modified residue7271Phosphoserine Ref.14 Ref.15
Modified residue7361Phosphoserine Ref.11
Modified residue7401Phosphoserine Ref.11
Modified residue10621Phosphoserine Ref.15
Modified residue11941Phosphoserine Ref.11
Modified residue12221Phosphoserine Ref.13 Ref.15
Modified residue12521Phosphoserine Ref.14
Modified residue12611Phosphoserine Ref.15
Modified residue12681Phosphoserine Ref.9 Ref.13 Ref.14 Ref.15
Modified residue12781Phosphoserine Ref.9 Ref.13 Ref.14 Ref.15
Modified residue12831Phosphoserine Ref.9
Modified residue12871Phosphoserine Ref.11 Ref.14
Modified residue13331Phosphoserine Ref.14
Modified residue13801Phosphoserine Ref.9 Ref.11 Ref.15
Modified residue13821Phosphoserine Ref.9 Ref.11 Ref.15
Modified residue14391Phosphothreonine Ref.11
Modified residue14411Phosphothreonine Ref.11
Modified residue16331Phosphothreonine Ref.14
Modified residue18971Phosphoserine Ref.11 Ref.14
Modified residue19471Phosphothreonine Ref.13
Modified residue21011Phosphoserine Ref.14 Ref.15
Modified residue21201Phosphoserine Ref.11 Ref.14 Ref.15
Modified residue21261Phosphoserine Ref.11
Modified residue21591Phosphoserine Ref.14
Modified residue23661Phosphoserine Ref.11
Modified residue24211Phosphothreonine Ref.11
Modified residue24521Phosphoserine Ref.13
Modified residue24601Phosphothreonine Ref.13
Modified residue29381Phosphothreonine Ref.11
Modified residue29501Phosphothreonine Ref.11
Modified residue34331Phosphoserine Ref.11

Natural variations

Natural variant9701A → V.
Corresponds to variant rs848208 [ dbSNP | Ensembl ].
VAR_017119
Natural variant9901D → H in a breast cancer sample; somatic mutation. Ref.17
VAR_035483
Natural variant10911L → P. Ref.4
Corresponds to variant rs848209 [ dbSNP | Ensembl ].
VAR_017120
Natural variant13631D → E.
Corresponds to variant rs12095818 [ dbSNP | Ensembl ].
VAR_052208
Natural variant14881R → I in a breast cancer sample; somatic mutation. Ref.17
VAR_035484
Natural variant23601N → D.
Corresponds to variant rs848210 [ dbSNP | Ensembl ].
VAR_017121

Experimental info

Sequence conflict9561G → D Ref.4

Secondary structure

..................................... 3664
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96T58 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 5228C58533E5B27B

FASTA3,664402,248
        10         20         30         40         50         60 
MVRETRHLWV GNLPENVREE KIIEHFKRYG RVESVKILPK RGSEGGVAAF VDFVDIKSAQ 

        70         80         90        100        110        120 
KAHNSVNKMG DRDLRTDYNE PGTIPSAARG LDDTVSIASR SREVSGFRGG GGGPAYGPPP 

       130        140        150        160        170        180 
SLHAREGRYE RRLDGASDNR ERAYEHSAYG HHERGTGGFD RTRHYDQDYY RDPRERTLQH 

       190        200        210        220        230        240 
GLYYASRSRS PNRFDAHDPR YEPRAREQFT LPSVVHRDIY RDDITREVRG RRPERNYQHS 

       250        260        270        280        290        300 
RSRSPHSSQS RNQSPQRLAS QASRPTRSPS GSGSRSRSSS SDSISSSSST SSDSSDSSSS 

       310        320        330        340        350        360 
SSDDSPARSV QSAAVPAPTS QLLSSLEKDE PRKSFGIKVQ NLPVRSTDTS LKDGLFHEFK 

       370        380        390        400        410        420 
KFGKVTSVQI HGTSEERYGL VFFRQQEDQE KALTASKGKL FFGMQIEVTA WIGPETESEN 

       430        440        450        460        470        480 
EFRPLDERID EFHPKATRTL FIGNLEKTTT YHDLRNIFQR FGEIVDIDIK KVNGVPQYAF 

       490        500        510        520        530        540 
LQYCDIASVC KAIKKMDGEY LGNNRLKLGF GKSMPTNCVW LDGLSSNVSD QYLTRHFCRY 

       550        560        570        580        590        600 
GPVVKVVFDR LKGMALVLYN EIEYAQAAVK ETKGRKIGGN KIKVDFANRE SQLAFYHCME 

       610        620        630        640        650        660 
KSGQDIRDFY EMLAERREER RASYDYNQDR TYYESVRTPG TYPEDSRRDY PARGREFYSE 

       670        680        690        700        710        720 
WETYQGDYYE SRYYDDPREY RDYRNDPYEQ DIREYSYRQR ERERERERFE SDRDRDHERR 

       730        740        750        760        770        780 
PIERSQSPVH LRRPQSPGAS PSQAERLPSD SERRLYSRSS DRSGSCSSLS PPRYEKLDKS 

       790        800        810        820        830        840 
RLERYTKNEK TDKERTFDPE RVERERRLIR KEKVEKDKTD KQKRKGKVHS PSSQSSETDQ 

       850        860        870        880        890        900 
ENEREQSPEK PRSCNKLSRE KADKEGIAKN RLELMPCVVL TRVKEKEGKV IDHTPVEKLK 

       910        920        930        940        950        960 
AKLDNDTVKS SALDQKLQVS QTEPAKSDLS KLESVRMKVP KEKGLSSHVE VVEKEGRLKA 

       970        980        990       1000       1010       1020 
RKHLKPEQPA DGVSAVDLEK LEARKRRFAD SNLKAEKQKP EVKKSSPEME DARVLSKKQP 

      1030       1040       1050       1060       1070       1080 
DVSSREVILL REGEAERKPV RKEILKRESK KIKLDRLNTV ASPKDCQELA SISVGSGSRP 

      1090       1100       1110       1120       1130       1140 
SSDLQARLGE LAGESVENQE VQSKKPIPSK PQLKQLQVLD DQGPEREDVR KNYCSLRDET 

      1150       1160       1170       1180       1190       1200 
PERKSGQEKS HSVNTEEKIG IDIDHTQSYR KQMEQSRRKQ QMEMEIAKSE KFGSPKKDVD 

      1210       1220       1230       1240       1250       1260 
EYERRSLVHE VGKPPQDVTD DSPPSKKKRM DHVDFDICTK RERNYRSSRQ ISEDSERTGG 

      1270       1280       1290       1300       1310       1320 
SPSVRHGSFH EDEDPIGSPR LLSVKGSPKV DEKVLPYSNI TVREESLKFN PYDSSRREQM 

      1330       1340       1350       1360       1370       1380 
ADMAKIKLSV LNSEDELNRW DSQMKQDAGR FDVSFPNSII KRDSLRKRSV RDLEPGEVPS 

      1390       1400       1410       1420       1430       1440 
DSDEDGEHKS HSPRASALYE SSRLSFLLRD REDKLRERDE RLSSSLERNK FYSFALDKTI 

      1450       1460       1470       1480       1490       1500 
TPDTKALLER AKSLSSSREE NWSFLDWDSR FANFRNNKDK EKVDSAPRPI PSWYMKKKKI 

      1510       1520       1530       1540       1550       1560 
RTDSEGKMDD KKEDHKEEEQ ERQELFASRF LHSSIFEQDS KRLQHLERKE EDSDFISGRI 

      1570       1580       1590       1600       1610       1620 
YGKQTSEGAN STTDSIQEPV VLFHSRFMEL TRMQQKEKEK DQKPKEVEKQ EDTENHPKTP 

      1630       1640       1650       1660       1670       1680 
ESAPENKDSE LKTPPSVGPP SVTVVTLESA PSALEKTTGD KTVEAPLVTE EKTVEPATVS 

      1690       1700       1710       1720       1730       1740 
EEAKPASEPA PAPVEQLEQV DLPPGADPDK EAAMMPAGVE EGSSGDQPPY LDAKPPTPGA 

      1750       1760       1770       1780       1790       1800 
SFSQAESNVD PEPDSTQPLS KPAQKSEEAN EPKAEKPDAT ADAEPDANQK AEAAPESQPP 

      1810       1820       1830       1840       1850       1860 
ASEDLEVDPP VAAKDKKPNK SKRSKTPVQA AAVSIVEKPV TRKSERIDRE KLKRSNSPRG 

      1870       1880       1890       1900       1910       1920 
EAQKLLELKM EAEKITRTAS KNSAADLEHP EPSLPLSRTR RRNVRSVYAT MGDHENRSPV 

      1930       1940       1950       1960       1970       1980 
KEPVEQPRVT RKRLERELQE AAAVPTTPRR GRPPKTRRRA DEEEENEAKE PAETLKPPEG 

      1990       2000       2010       2020       2030       2040 
WRSPRSQKTA AGGGPQGKKG KNEPKVDATR PEATTEVGPQ IGVKESSMEP KAAEEEAGSE 

      2050       2060       2070       2080       2090       2100 
QKRDRKDAGT DKNPPETAPV EVVEKKPAPE KNSKSKRGRS RNSRLAVDKS ASLKNVDAAV 

      2110       2120       2130       2140       2150       2160 
SPRGAAAQAG ERESGVVAVS PEKSESPQKE DGLSSQLKSD PVDPDKEPEK EDVSASGPSP 

      2170       2180       2190       2200       2210       2220 
EATQLAKQME LEQAVEHIAK LAEASASAAY KADAPEGLAP EDRDKPAHQA SETELAAAIG 

      2230       2240       2250       2260       2270       2280 
SIINDISGEP ENFPAPPPYP GESQTDLQPP AGAQALQPSE EGMETDEAVS GILETEAATE 

      2290       2300       2310       2320       2330       2340 
SSRPPVNAPD PSAGPTDTKE ARGNSSETSH SVPEAKGSKE VEVTLVRKDK GRQKTTRSRR 

      2350       2360       2370       2380       2390       2400 
KRNTNKKVVA PVESHVPESN QAQGESPAAN EGTTVQHPEA PQEEKQSEKP HSTPPQSCTS 

      2410       2420       2430       2440       2450       2460 
DLSKIPSTEN SSQEISVEER TPTKASVPPD LPPPPQPAPV DEEPQARFRV HSIIESDPVT 

      2470       2480       2490       2500       2510       2520 
PPSDPSIPIP TLPSVTAAKL SPPVASGGIP HQSPPTKVTE WITRQEEPRA QSTPSPALPP 

      2530       2540       2550       2560       2570       2580 
DTKASDVDTS SSTLRKILMD PKYVSATSVT STSVTTAIAE PVSAAPCLHE APPPPVDSKK 

      2590       2600       2610       2620       2630       2640 
PLEEKTAPPV TNNSEIQASE VLVAADKEKV APVIAPKITS VISRMPVSID LENSQKITLA 

      2650       2660       2670       2680       2690       2700 
KPAPQTLTGL VSALTGLVNV SLVPVNALKG PVKGSVTTLK SLVSTPAGPV NVLKGPVNVL 

      2710       2720       2730       2740       2750       2760 
TGPVNVLTTP VNATVGTVNA APGTVNAAAS AVNATASAVT VTAGAVTAAS GGVTATTGTV 

      2770       2780       2790       2800       2810       2820 
TMAGAVIAPS TKCKQRASAN ENSRFHPGSM PVIDDRPADA GSGAGLRVNT SEGVVLLSYS 

      2830       2840       2850       2860       2870       2880 
GQKTEGPQRI SAKISQIPPA SAMDIEFQQS VSKSQVKPDS VTASQPPSKG PQAPAGYANV 

      2890       2900       2910       2920       2930       2940 
ATHSTLVLTA QTYNASPVIS SVKADRPSLE KPEPIHLSVS TPVTQGGTVK VLTQGINTPP 

      2950       2960       2970       2980       2990       3000 
VLVHNQLVLT PSIVTTNKKL ADPVTLKIET KVLQPANLGS TLTPHHPPAL PSKLPTEVNH 

      3010       3020       3030       3040       3050       3060 
VPSGPSIPAD RTVSHLAAAK LDAHSPRPSG PGPSSFPRAS HPSSTASTAL STNATVMLAA 

      3070       3080       3090       3100       3110       3120 
GIPVPQFISS IHPEQSVIMP PHSITQTVSL SHLSQGEVRM NTPTLPSITY SIRPEALHSP 

      3130       3140       3150       3160       3170       3180 
RAPLQPQQIE VRAPQRASTP QPAPAGVPAL ASQHPPEEEV HYHLPVARAT APVQSEVLVM 

      3190       3200       3210       3220       3230       3240 
QSEYRLHPYT VPRDVRIMVH PHVTAVSEQP RAADGVVKVP PASKAPQQPG KEAAKTPDAK 

      3250       3260       3270       3280       3290       3300 
AAPTPTPAPV PVPVPLPAPA PAPHGEARIL TVTPSNQLQG LPLTPPVVVT HGVQIVHSSG 

      3310       3320       3330       3340       3350       3360 
ELFQEYRYGD IRTYHPPAQL THTQFPAASS VGLPSRTKTA AQGPPPEGEP LQPPQPVQST 

      3370       3380       3390       3400       3410       3420 
QPAQPAPPCP PSQLGQPGQP PSSKMPQVSQ EAKGTQTGVE QPRLPAGPAN RPPEPHTQVQ 

      3430       3440       3450       3460       3470       3480 
RAQAETGPTS FPSPVSVSMK PDLPVSLPTQ TAPKQPLFVP TTSGPSTPPG LVLPHTEFQP 

      3490       3500       3510       3520       3530       3540 
APKQDSSPHL TSQRPVDMVQ LLKKYPIVWQ GLLALKNDTA AVQLHFVSGN NVLAHRSLPL 

      3550       3560       3570       3580       3590       3600 
SEGGPPLRIA QRMRLEATQL EGVARRMTVE TDYCLLLALP CGRDQEDVVS QTESLKAAFI 

      3610       3620       3630       3640       3650       3660 
TYLQAKQAAG IINVPNPGSN QPAYVLQIFP PCEFSESHLS RLAPDLLASI SNISPHLMIV 


IASV 

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References

« Hide 'large scale' references
[1]"Sharp, an inducible cofactor that integrates nuclear receptor repression and activation."
Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.
Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, RNA-BINDING, INTERACTION WITH NCOR2; HDAC1; HDAC2; RBBP4; MBD3; RAR AND MTA1L1.
Tissue: Liver and Pituitary.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Rhodes S., Huckle E.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 294-3664.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 793-1595, VARIANT PRO-1091.
Tissue: Embryo and Teratocarcinoma.
[5]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2002-3664.
Tissue: Brain.
[6]"The peroxisome proliferator-activated receptor delta, an integrator of transcriptional repression and nuclear receptor signaling."
Shi Y., Hon M., Evans R.M.
Proc. Natl. Acad. Sci. U.S.A. 99:2613-2618(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPARD.
[7]"SHARP is a novel component of the Notch/RBP-Jkappa signalling pathway."
Oswald F., Kostezka U., Astrahantseff K., Bourteele S., Dillinger K., Zechner U., Ludwig L., Wilda M., Hameister H., Knoechel W., Liptay S., Schmid R.M.
EMBO J. 21:5417-5426(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RBPSUH.
[8]"Interaction of the Epstein-Barr virus mRNA export factor EB2 with human Spen proteins SHARP, OTT1, and a novel member of the family, OTT3, links Spen proteins with splicing regulation and mRNA export."
Hiriart E., Gruffat H., Buisson M., Mikaelian I., Keppler S., Meresse P., Mercher T., Bernard O.A., Sergeant A., Manet E.
J. Biol. Chem. 280:36935-36945(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EBV BSFL2/BMLF1.
[9]"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-1268; SER-1278; SER-1283; SER-1380 AND SER-1382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"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-736; SER-740; SER-1194; SER-1287; SER-1380; SER-1382; THR-1439; THR-1441; SER-1897; SER-2120; SER-2126; SER-2366; THR-2421; THR-2938; THR-2950 AND SER-3433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222; SER-1268; SER-1278; THR-1947; SER-2452 AND THR-2460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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-309; SER-623; SER-727; SER-1252; SER-1268; SER-1278; SER-1287; SER-1333; THR-1633; SER-1897; SER-2101; SER-2120 AND SER-2159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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-727; SER-1062; SER-1222; SER-1261; SER-1268; SER-1278; SER-1380; SER-1382; SER-2101 AND SER-2120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signaling."
Ariyoshi M., Schwabe J.W.R.
Genes Dev. 17:1909-1920(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF SPOC DOMAIN.
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-990 AND ILE-1488.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF356524 mRNA. Translation: AAK52750.1.
AL034555, AL450998 Genomic DNA. Translation: CAI19526.1.
AL450998, AL034555 Genomic DNA. Translation: CAH70858.1.
AL096858 mRNA. Translation: CAB51072.1. Different initiation.
AK000882 mRNA. Translation: BAA91405.1. Different initiation.
AK022949 mRNA. Translation: BAB14324.1. Different initiation.
AB023146 mRNA. Translation: BAA76773.1.
CCDSCCDS164.1.
RefSeqNP_055816.2. NM_015001.2.
UniGeneHs.744843.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OW1X-ray1.80A3470-3664[»]
2RT5NMR-A3496-3664[»]
4P6QX-ray2.00A335-620[»]
ProteinModelPortalQ96T58.
SMRQ96T58. Positions 438-589, 3496-3664.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116655. 30 interactions.
DIPDIP-34569N.
IntActQ96T58. 21 interactions.
STRING9606.ENSP00000364912.

PTM databases

PhosphoSiteQ96T58.

Polymorphism databases

DMDM41688816.

Proteomic databases

MaxQBQ96T58.
PaxDbQ96T58.
PRIDEQ96T58.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375759; ENSP00000364912; ENSG00000065526.
GeneID23013.
KEGGhsa:23013.
UCSCuc001axk.1. human.

Organism-specific databases

CTD23013.
GeneCardsGC01P016174.
H-InvDBHIX0159662.
HGNCHGNC:17575. SPEN.
HPAHPA015825.
HPA050257.
MIM613484. gene.
neXtProtNX_Q96T58.
PharmGKBPA134895302.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000231295.
HOVERGENHBG045583.
InParanoidQ96T58.
OMADKGRQKT.
OrthoDBEOG7QNVK1.
PhylomeDBQ96T58.
TreeFamTF315637.

Gene expression databases

ArrayExpressQ96T58.
BgeeQ96T58.
CleanExHS_SPEN.
GenevestigatorQ96T58.

Family and domain databases

Gene3D2.40.290.10. 1 hit.
3.30.70.330. 4 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR012921. SPOC_C.
IPR016194. SPOC_like_C_dom.
IPR010912. SPOC_met.
[Graphical view]
PfamPF00076. RRM_1. 3 hits.
PF07744. SPOC. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 4 hits.
[Graphical view]
SUPFAMSSF100939. SSF100939. 1 hit.
PROSITEPS50102. RRM. 4 hits.
PS50917. SPOC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSPEN. human.
EvolutionaryTraceQ96T58.
GeneWikiSPEN.
GenomeRNAi23013.
NextBio43936.
PROQ96T58.
SOURCESearch...

Entry information

Entry nameMINT_HUMAN
AccessionPrimary (citable) accession number: Q96T58
Secondary accession number(s): Q9H9A8 expand/collapse secondary AC list , Q9NWH5, Q9UQ01, Q9Y556
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 139 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 1

Human chromosome 1: entries, gene names and cross-references to MIM