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Q96T58

- MINT_HUMAN

UniProt

Q96T58 - MINT_HUMAN

Protein

Msx2-interacting protein

Gene

SPEN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    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.By similarity2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi1 – 573573By similarityAdd
    BLAST

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. RNA polymerase II transcription factor binding Source: BHF-UCL
    5. RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription Source: BHF-UCL
    6. sequence-specific DNA binding transcription factor activity Source: Ensembl
    7. single-stranded DNA binding Source: Ensembl
    8. transcription corepressor activity Source: Ensembl

    GO - Biological processi

    1. negative regulation of transcription, DNA-templated Source: UniProtKB
    2. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    3. Notch signaling pathway Source: UniProtKB-KW
    4. positive regulation of neurogenesis Source: BHF-UCL
    5. positive regulation of transcription, DNA-templated Source: Ensembl
    6. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Host-virus interaction, Notch signaling pathway, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Msx2-interacting protein
    Alternative name(s):
    SMART/HDAC1-associated repressor protein
    SPEN homolog
    Gene namesi
    Name:SPEN
    Synonyms:KIAA0929, MINT, SHARP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:17575. SPEN.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Associates with chromatin.

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. nucleus Source: HPA
    3. transcriptional repressor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134895302.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 36643664Msx2-interacting proteinPRO_0000081627Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei309 – 3091Phosphoserine1 Publication
    Modified residuei623 – 6231Phosphoserine1 Publication
    Modified residuei727 – 7271Phosphoserine2 Publications
    Modified residuei736 – 7361Phosphoserine1 Publication
    Modified residuei740 – 7401Phosphoserine1 Publication
    Modified residuei1062 – 10621Phosphoserine1 Publication
    Modified residuei1194 – 11941Phosphoserine1 Publication
    Modified residuei1222 – 12221Phosphoserine2 Publications
    Modified residuei1252 – 12521Phosphoserine1 Publication
    Modified residuei1261 – 12611Phosphoserine1 Publication
    Modified residuei1268 – 12681Phosphoserine4 Publications
    Modified residuei1278 – 12781Phosphoserine4 Publications
    Modified residuei1283 – 12831Phosphoserine1 Publication
    Modified residuei1287 – 12871Phosphoserine2 Publications
    Modified residuei1333 – 13331Phosphoserine1 Publication
    Modified residuei1380 – 13801Phosphoserine3 Publications
    Modified residuei1382 – 13821Phosphoserine3 Publications
    Modified residuei1439 – 14391Phosphothreonine1 Publication
    Modified residuei1441 – 14411Phosphothreonine1 Publication
    Modified residuei1633 – 16331Phosphothreonine1 Publication
    Modified residuei1897 – 18971Phosphoserine2 Publications
    Modified residuei1947 – 19471Phosphothreonine1 Publication
    Modified residuei2101 – 21011Phosphoserine2 Publications
    Modified residuei2120 – 21201Phosphoserine3 Publications
    Modified residuei2126 – 21261Phosphoserine1 Publication
    Modified residuei2159 – 21591Phosphoserine1 Publication
    Modified residuei2366 – 23661Phosphoserine1 Publication
    Modified residuei2421 – 24211Phosphothreonine1 Publication
    Modified residuei2452 – 24521Phosphoserine1 Publication
    Modified residuei2460 – 24601Phosphothreonine1 Publication
    Modified residuei2938 – 29381Phosphothreonine1 Publication
    Modified residuei2950 – 29501Phosphothreonine1 Publication
    Modified residuei3433 – 34331Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96T58.
    PaxDbiQ96T58.
    PRIDEiQ96T58.

    PTM databases

    PhosphoSiteiQ96T58.

    Expressioni

    Tissue specificityi

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

    Inductioni

    By 17-beta-estradiol.1 Publication

    Gene expression databases

    ArrayExpressiQ96T58.
    BgeeiQ96T58.
    CleanExiHS_SPEN.
    GenevestigatoriQ96T58.

    Organism-specific databases

    HPAiHPA015825.
    HPA050257.

    Interactioni

    Subunit structurei

    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.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK1P163333EBI-765739,EBI-389883

    Protein-protein interaction databases

    BioGridi116655. 30 interactions.
    DIPiDIP-34569N.
    IntActiQ96T58. 21 interactions.
    STRINGi9606.ENSP00000364912.

    Structurei

    Secondary structure

    1
    3664
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi336 – 3405
    Helixi348 – 35912
    Helixi360 – 3623
    Beta strandi365 – 3717
    Turni374 – 3763
    Beta strandi378 – 3858
    Helixi386 – 39510
    Turni396 – 3983
    Beta strandi407 – 4104
    Helixi414 – 4229
    Beta strandi438 – 4447
    Helixi451 – 4588
    Beta strandi464 – 4729
    Beta strandi475 – 48511
    Helixi486 – 49611
    Beta strandi507 – 5104
    Beta strandi517 – 5226
    Helixi530 – 5378
    Helixi538 – 5403
    Beta strandi543 – 5497
    Turni550 – 5534
    Beta strandi554 – 5607
    Helixi562 – 57211
    Beta strandi575 – 5773
    Beta strandi583 – 5864
    Helixi589 – 60113
    Helixi609 – 61810
    Helixi3501 – 35044
    Beta strandi3507 – 35159
    Beta strandi3518 – 352912
    Helixi3531 – 35377
    Beta strandi3541 – 35433
    Beta strandi3547 – 35493
    Beta strandi3551 – 35544
    Helixi3557 – 356610
    Turni3570 – 35723
    Beta strandi3573 – 35808
    Helixi3585 – 359814
    Helixi3600 – 36067
    Beta strandi3608 – 36147
    Turni3617 – 36193
    Beta strandi3624 – 36296
    Helixi3633 – 364210
    Helixi3644 – 36507
    Turni3651 – 36533
    Beta strandi3657 – 36637

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OW1X-ray1.80A3470-3664[»]
    2RT5NMR-A3496-3664[»]
    4P6QX-ray2.00A335-620[»]
    ProteinModelPortaliQ96T58.
    SMRiQ96T58. Positions 438-589, 3496-3664.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96T58.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 8176RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini335 – 41581RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini438 – 51376RRM 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini517 – 58973RRM 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini2201 – 2707507RIDAdd
    BLAST
    Domaini3498 – 3664167SPOCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2130 – 2464335Interaction with MSX2By similarityAdd
    BLAST
    Regioni2709 – 2870162Interaction with RBPSUHBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili688 – 71528Sequence AnalysisAdd
    BLAST
    Coiled coili977 – 100428Sequence AnalysisAdd
    BLAST
    Coiled coili1170 – 119122Sequence AnalysisAdd
    BLAST
    Coiled coili1408 – 142821Sequence AnalysisAdd
    BLAST
    Coiled coili1496 – 152934Sequence AnalysisAdd
    BLAST
    Coiled coili1592 – 161221Sequence AnalysisAdd
    BLAST
    Coiled coili1928 – 194417Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi125 – 277153Arg-richAdd
    BLAST
    Compositional biasi240 – 32586Ser-richAdd
    BLAST
    Compositional biasi616 – 810195Arg-richAdd
    BLAST
    Compositional biasi624 – 69774Tyr-richAdd
    BLAST
    Compositional biasi2428 – 252093Pro-richAdd
    BLAST
    Compositional biasi3220 – 3482263Pro-richAdd
    BLAST

    Domaini

    The RID domain mediates the interaction with nuclear receptors.By similarity
    The SPOC domain, which mediates the interaction with NCOR2, is essential for the repressive activity.

    Sequence similaritiesi

    Belongs to the RRM Spen family.Curated
    Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation
    Contains 1 SPOC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000231295.
    HOVERGENiHBG045583.
    InParanoidiQ96T58.
    OMAiDKGRQKT.
    OrthoDBiEOG7QNVK1.
    PhylomeDBiQ96T58.
    TreeFamiTF315637.

    Family and domain databases

    Gene3Di2.40.290.10. 1 hit.
    3.30.70.330. 4 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR012921. SPOC_C.
    IPR016194. SPOC_like_C_dom.
    IPR010912. SPOC_met.
    [Graphical view]
    PfamiPF00076. RRM_1. 3 hits.
    PF07744. SPOC. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 4 hits.
    [Graphical view]
    SUPFAMiSSF100939. SSF100939. 1 hit.
    PROSITEiPS50102. RRM. 4 hits.
    PS50917. SPOC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q96T58-1 [UniParc]FASTAAdd to Basket

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    MVRETRHLWV GNLPENVREE KIIEHFKRYG RVESVKILPK RGSEGGVAAF     50
    VDFVDIKSAQ KAHNSVNKMG DRDLRTDYNE PGTIPSAARG LDDTVSIASR 100
    SREVSGFRGG GGGPAYGPPP SLHAREGRYE RRLDGASDNR ERAYEHSAYG 150
    HHERGTGGFD RTRHYDQDYY RDPRERTLQH GLYYASRSRS PNRFDAHDPR 200
    YEPRAREQFT LPSVVHRDIY RDDITREVRG RRPERNYQHS RSRSPHSSQS 250
    RNQSPQRLAS QASRPTRSPS GSGSRSRSSS SDSISSSSST SSDSSDSSSS 300
    SSDDSPARSV QSAAVPAPTS QLLSSLEKDE PRKSFGIKVQ NLPVRSTDTS 350
    LKDGLFHEFK KFGKVTSVQI HGTSEERYGL VFFRQQEDQE KALTASKGKL 400
    FFGMQIEVTA WIGPETESEN EFRPLDERID EFHPKATRTL FIGNLEKTTT 450
    YHDLRNIFQR FGEIVDIDIK KVNGVPQYAF LQYCDIASVC KAIKKMDGEY 500
    LGNNRLKLGF GKSMPTNCVW LDGLSSNVSD QYLTRHFCRY GPVVKVVFDR 550
    LKGMALVLYN EIEYAQAAVK ETKGRKIGGN KIKVDFANRE SQLAFYHCME 600
    KSGQDIRDFY EMLAERREER RASYDYNQDR TYYESVRTPG TYPEDSRRDY 650
    PARGREFYSE WETYQGDYYE SRYYDDPREY RDYRNDPYEQ DIREYSYRQR 700
    ERERERERFE SDRDRDHERR PIERSQSPVH LRRPQSPGAS PSQAERLPSD 750
    SERRLYSRSS DRSGSCSSLS PPRYEKLDKS RLERYTKNEK TDKERTFDPE 800
    RVERERRLIR KEKVEKDKTD KQKRKGKVHS PSSQSSETDQ ENEREQSPEK 850
    PRSCNKLSRE KADKEGIAKN RLELMPCVVL TRVKEKEGKV IDHTPVEKLK 900
    AKLDNDTVKS SALDQKLQVS QTEPAKSDLS KLESVRMKVP KEKGLSSHVE 950
    VVEKEGRLKA RKHLKPEQPA DGVSAVDLEK LEARKRRFAD SNLKAEKQKP 1000
    EVKKSSPEME DARVLSKKQP DVSSREVILL REGEAERKPV RKEILKRESK 1050
    KIKLDRLNTV ASPKDCQELA SISVGSGSRP SSDLQARLGE LAGESVENQE 1100
    VQSKKPIPSK PQLKQLQVLD DQGPEREDVR KNYCSLRDET PERKSGQEKS 1150
    HSVNTEEKIG IDIDHTQSYR KQMEQSRRKQ QMEMEIAKSE KFGSPKKDVD 1200
    EYERRSLVHE VGKPPQDVTD DSPPSKKKRM DHVDFDICTK RERNYRSSRQ 1250
    ISEDSERTGG SPSVRHGSFH EDEDPIGSPR LLSVKGSPKV DEKVLPYSNI 1300
    TVREESLKFN PYDSSRREQM ADMAKIKLSV LNSEDELNRW DSQMKQDAGR 1350
    FDVSFPNSII KRDSLRKRSV RDLEPGEVPS DSDEDGEHKS HSPRASALYE 1400
    SSRLSFLLRD REDKLRERDE RLSSSLERNK FYSFALDKTI TPDTKALLER 1450
    AKSLSSSREE NWSFLDWDSR FANFRNNKDK EKVDSAPRPI PSWYMKKKKI 1500
    RTDSEGKMDD KKEDHKEEEQ ERQELFASRF LHSSIFEQDS KRLQHLERKE 1550
    EDSDFISGRI YGKQTSEGAN STTDSIQEPV VLFHSRFMEL TRMQQKEKEK 1600
    DQKPKEVEKQ EDTENHPKTP ESAPENKDSE LKTPPSVGPP SVTVVTLESA 1650
    PSALEKTTGD KTVEAPLVTE EKTVEPATVS EEAKPASEPA PAPVEQLEQV 1700
    DLPPGADPDK EAAMMPAGVE EGSSGDQPPY LDAKPPTPGA SFSQAESNVD 1750
    PEPDSTQPLS KPAQKSEEAN EPKAEKPDAT ADAEPDANQK AEAAPESQPP 1800
    ASEDLEVDPP VAAKDKKPNK SKRSKTPVQA AAVSIVEKPV TRKSERIDRE 1850
    KLKRSNSPRG EAQKLLELKM EAEKITRTAS KNSAADLEHP EPSLPLSRTR 1900
    RRNVRSVYAT MGDHENRSPV KEPVEQPRVT RKRLERELQE AAAVPTTPRR 1950
    GRPPKTRRRA DEEEENEAKE PAETLKPPEG WRSPRSQKTA AGGGPQGKKG 2000
    KNEPKVDATR PEATTEVGPQ IGVKESSMEP KAAEEEAGSE QKRDRKDAGT 2050
    DKNPPETAPV EVVEKKPAPE KNSKSKRGRS RNSRLAVDKS ASLKNVDAAV 2100
    SPRGAAAQAG ERESGVVAVS PEKSESPQKE DGLSSQLKSD PVDPDKEPEK 2150
    EDVSASGPSP EATQLAKQME LEQAVEHIAK LAEASASAAY KADAPEGLAP 2200
    EDRDKPAHQA SETELAAAIG SIINDISGEP ENFPAPPPYP GESQTDLQPP 2250
    AGAQALQPSE EGMETDEAVS GILETEAATE SSRPPVNAPD PSAGPTDTKE 2300
    ARGNSSETSH SVPEAKGSKE VEVTLVRKDK GRQKTTRSRR KRNTNKKVVA 2350
    PVESHVPESN QAQGESPAAN EGTTVQHPEA PQEEKQSEKP HSTPPQSCTS 2400
    DLSKIPSTEN SSQEISVEER TPTKASVPPD LPPPPQPAPV DEEPQARFRV 2450
    HSIIESDPVT PPSDPSIPIP TLPSVTAAKL SPPVASGGIP HQSPPTKVTE 2500
    WITRQEEPRA QSTPSPALPP DTKASDVDTS SSTLRKILMD PKYVSATSVT 2550
    STSVTTAIAE PVSAAPCLHE APPPPVDSKK PLEEKTAPPV TNNSEIQASE 2600
    VLVAADKEKV APVIAPKITS VISRMPVSID LENSQKITLA KPAPQTLTGL 2650
    VSALTGLVNV SLVPVNALKG PVKGSVTTLK SLVSTPAGPV NVLKGPVNVL 2700
    TGPVNVLTTP VNATVGTVNA APGTVNAAAS AVNATASAVT VTAGAVTAAS 2750
    GGVTATTGTV TMAGAVIAPS TKCKQRASAN ENSRFHPGSM PVIDDRPADA 2800
    GSGAGLRVNT SEGVVLLSYS GQKTEGPQRI SAKISQIPPA SAMDIEFQQS 2850
    VSKSQVKPDS VTASQPPSKG PQAPAGYANV ATHSTLVLTA QTYNASPVIS 2900
    SVKADRPSLE KPEPIHLSVS TPVTQGGTVK VLTQGINTPP VLVHNQLVLT 2950
    PSIVTTNKKL ADPVTLKIET KVLQPANLGS TLTPHHPPAL PSKLPTEVNH 3000
    VPSGPSIPAD RTVSHLAAAK LDAHSPRPSG PGPSSFPRAS HPSSTASTAL 3050
    STNATVMLAA GIPVPQFISS IHPEQSVIMP PHSITQTVSL SHLSQGEVRM 3100
    NTPTLPSITY SIRPEALHSP RAPLQPQQIE VRAPQRASTP QPAPAGVPAL 3150
    ASQHPPEEEV HYHLPVARAT APVQSEVLVM QSEYRLHPYT VPRDVRIMVH 3200
    PHVTAVSEQP RAADGVVKVP PASKAPQQPG KEAAKTPDAK AAPTPTPAPV 3250
    PVPVPLPAPA PAPHGEARIL TVTPSNQLQG LPLTPPVVVT HGVQIVHSSG 3300
    ELFQEYRYGD IRTYHPPAQL THTQFPAASS VGLPSRTKTA AQGPPPEGEP 3350
    LQPPQPVQST QPAQPAPPCP PSQLGQPGQP PSSKMPQVSQ EAKGTQTGVE 3400
    QPRLPAGPAN RPPEPHTQVQ RAQAETGPTS FPSPVSVSMK PDLPVSLPTQ 3450
    TAPKQPLFVP TTSGPSTPPG LVLPHTEFQP APKQDSSPHL TSQRPVDMVQ 3500
    LLKKYPIVWQ GLLALKNDTA AVQLHFVSGN NVLAHRSLPL SEGGPPLRIA 3550
    QRMRLEATQL EGVARRMTVE TDYCLLLALP CGRDQEDVVS QTESLKAAFI 3600
    TYLQAKQAAG IINVPNPGSN QPAYVLQIFP PCEFSESHLS RLAPDLLASI 3650
    SNISPHLMIV IASV 3664
    Length:3,664
    Mass (Da):402,248
    Last modified:December 1, 2001 - v1
    Checksum:i5228C58533E5B27B
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti956 – 9561G → D(PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti970 – 9701A → V.
    Corresponds to variant rs848208 [ dbSNP | Ensembl ].
    VAR_017119
    Natural varianti990 – 9901D → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035483
    Natural varianti1091 – 10911L → P.1 Publication
    Corresponds to variant rs848209 [ dbSNP | Ensembl ].
    VAR_017120
    Natural varianti1363 – 13631D → E.
    Corresponds to variant rs12095818 [ dbSNP | Ensembl ].
    VAR_052208
    Natural varianti1488 – 14881R → I in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035484
    Natural varianti2360 – 23601N → D.
    Corresponds to variant rs848210 [ dbSNP | Ensembl ].
    VAR_017121

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS164.1.
    RefSeqiNP_055816.2. NM_015001.2.
    UniGeneiHs.744843.

    Genome annotation databases

    EnsembliENST00000375759; ENSP00000364912; ENSG00000065526.
    GeneIDi23013.
    KEGGihsa:23013.
    UCSCiuc001axk.1. human.

    Polymorphism databases

    DMDMi41688816.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS164.1.
    RefSeqi NP_055816.2. NM_015001.2.
    UniGenei Hs.744843.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OW1 X-ray 1.80 A 3470-3664 [» ]
    2RT5 NMR - A 3496-3664 [» ]
    4P6Q X-ray 2.00 A 335-620 [» ]
    ProteinModelPortali Q96T58.
    SMRi Q96T58. Positions 438-589, 3496-3664.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116655. 30 interactions.
    DIPi DIP-34569N.
    IntActi Q96T58. 21 interactions.
    STRINGi 9606.ENSP00000364912.

    PTM databases

    PhosphoSitei Q96T58.

    Polymorphism databases

    DMDMi 41688816.

    Proteomic databases

    MaxQBi Q96T58.
    PaxDbi Q96T58.
    PRIDEi Q96T58.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375759 ; ENSP00000364912 ; ENSG00000065526 .
    GeneIDi 23013.
    KEGGi hsa:23013.
    UCSCi uc001axk.1. human.

    Organism-specific databases

    CTDi 23013.
    GeneCardsi GC01P016174.
    H-InvDB HIX0159662.
    HGNCi HGNC:17575. SPEN.
    HPAi HPA015825.
    HPA050257.
    MIMi 613484. gene.
    neXtProti NX_Q96T58.
    PharmGKBi PA134895302.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000231295.
    HOVERGENi HBG045583.
    InParanoidi Q96T58.
    OMAi DKGRQKT.
    OrthoDBi EOG7QNVK1.
    PhylomeDBi Q96T58.
    TreeFami TF315637.

    Miscellaneous databases

    ChiTaRSi SPEN. human.
    EvolutionaryTracei Q96T58.
    GeneWikii SPEN.
    GenomeRNAii 23013.
    NextBioi 43936.
    PROi Q96T58.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96T58.
    Bgeei Q96T58.
    CleanExi HS_SPEN.
    Genevestigatori Q96T58.

    Family and domain databases

    Gene3Di 2.40.290.10. 1 hit.
    3.30.70.330. 4 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR012921. SPOC_C.
    IPR016194. SPOC_like_C_dom.
    IPR010912. SPOC_met.
    [Graphical view ]
    Pfami PF00076. RRM_1. 3 hits.
    PF07744. SPOC. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 4 hits.
    [Graphical view ]
    SUPFAMi SSF100939. SSF100939. 1 hit.
    PROSITEi PS50102. RRM. 4 hits.
    PS50917. SPOC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. 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. Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-990 AND ILE-1488.

    Entry informationi

    Entry nameiMINT_HUMAN
    AccessioniPrimary (citable) accession number: Q96T58
    Secondary accession number(s): Q9H9A8
    , Q9NWH5, Q9UQ01, Q9Y556
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 141 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3