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Q96T58

- MINT_HUMAN

UniProt

Q96T58 - MINT_HUMAN

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Protein
Msx2-interacting protein
Gene
SPEN, KIAA0929, MINT, SHARP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications

Regions

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

GO - Molecular functioni

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

GO - Biological processi

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

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
Note: Associates with chromatin.1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134895302.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 36643664Msx2-interacting protein
PRO_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/BMLF1.4 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

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.

Miscellaneous databases

EvolutionaryTraceiQ96T58.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 8176RRM 1
Add
BLAST
Domaini335 – 41581RRM 2
Add
BLAST
Domaini438 – 51376RRM 3
Add
BLAST
Domaini517 – 58973RRM 4
Add
BLAST
Domaini2201 – 2707507RID
Add
BLAST
Domaini3498 – 3664167SPOC
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2130 – 2464335Interaction with MSX2 By similarity
Add
BLAST
Regioni2709 – 2870162Interaction with RBPSUH By similarity
Add
BLAST

Coiled coil

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

Compositional bias

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

Domaini

The RID domain mediates the interaction with nuclear receptors By similarity.1 Publication
The SPOC domain, which mediates the interaction with NCOR2, is essential for the repressive activity.1 Publication

Sequence similaritiesi

Belongs to the RRM Spen family.
Contains 1 SPOC domain.

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

« Hide

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti956 – 9561G → D1 Publication

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...

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-InvDBi 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 140 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

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