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Protein

Msx2-interacting protein

Gene

SPEN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.By similarity2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi1 – 573By similarityAdd BLAST573

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • nucleic acid binding Source: GO_Central
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA polymerase II transcription factor binding Source: BHF-UCL
  • transcriptional repressor activity, RNA polymerase II transcription factor binding Source: BHF-UCL

GO - Biological processi

  • mRNA splicing, via spliceosome Source: GO_Central
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • Notch signaling pathway Source: UniProtKB-KW
  • positive regulation of neurogenesis Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
  • 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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000065526-MONOMER.
SIGNORiQ96T58.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17575. SPEN.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: GO_Central
  • transcriptional repressor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi23013.
OpenTargetsiENSG00000065526.
PharmGKBiPA134895302.

Polymorphism and mutation databases

BioMutaiSPEN.
DMDMi41688816.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000816271 – 3664Msx2-interacting proteinAdd BLAST3664

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei99PhosphoserineCombined sources1
Modified residuei108Omega-N-methylarginineCombined sources1
Modified residuei188PhosphoserineCombined sources1
Modified residuei190PhosphoserineCombined sources1
Modified residuei309PhosphoserineCombined sources1
Modified residuei623PhosphoserineCombined sources1
Modified residuei725PhosphoserineCombined sources1
Modified residuei727PhosphoserineCombined sources1
Modified residuei736PhosphoserineCombined sources1
Modified residuei740PhosphoserineCombined sources1
Modified residuei770PhosphoserineCombined sources1
Modified residuei830PhosphoserineBy similarity1
Modified residuei833PhosphoserineBy similarity1
Modified residuei847PhosphoserineCombined sources1
Modified residuei1062PhosphoserineCombined sources1
Modified residuei1140PhosphothreonineCombined sources1
Modified residuei1168PhosphoserineCombined sources1
Modified residuei1194PhosphoserineCombined sources1
Modified residuei1222PhosphoserineCombined sources1
Modified residuei1252PhosphoserineCombined sources1
Modified residuei1261PhosphoserineCombined sources1
Modified residuei1268PhosphoserineCombined sources1
Modified residuei1278PhosphoserineCombined sources1
Modified residuei1283PhosphoserineCombined sources1
Modified residuei1287PhosphoserineCombined sources1
Modified residuei1333PhosphoserineCombined sources1
Modified residuei1380PhosphoserineCombined sources1
Modified residuei1382PhosphoserineCombined sources1
Modified residuei1439PhosphothreonineCombined sources1
Modified residuei1441PhosphothreonineCombined sources1
Modified residuei1619PhosphothreonineCombined sources1
Modified residuei1633PhosphothreonineCombined sources1
Modified residuei1826PhosphothreonineCombined sources1
Modified residuei1897PhosphoserineCombined sources1
Modified residuei1918PhosphoserineCombined sources1
Modified residuei1947PhosphothreonineCombined sources1
Modified residuei2101PhosphoserineCombined sources1
Modified residuei2120PhosphoserineCombined sources1
Modified residuei2126PhosphoserineCombined sources1
Modified residuei2159PhosphoserineCombined sources1
Modified residuei2163PhosphothreonineCombined sources1
Modified residuei2366PhosphoserineCombined sources1
Modified residuei2393PhosphothreonineCombined sources1
Modified residuei2421PhosphothreonineCombined sources1
Modified residuei2452PhosphoserineCombined sources1
Modified residuei2456PhosphoserineCombined sources1
Modified residuei2460PhosphothreonineCombined sources1
Modified residuei2481PhosphoserineCombined sources1
Modified residuei2486PhosphoserineCombined sources1
Modified residuei2493PhosphoserineCombined sources1
Modified residuei2938PhosphothreonineCombined sources1
Modified residuei2950PhosphothreonineCombined sources1
Modified residuei3113Asymmetric dimethylarginineCombined sources1
Modified residuei3121Asymmetric dimethylarginineCombined sources1
Modified residuei3433PhosphoserineCombined sources1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ96T58.
MaxQBiQ96T58.
PaxDbiQ96T58.
PeptideAtlasiQ96T58.
PRIDEiQ96T58.

PTM databases

iPTMnetiQ96T58.
PhosphoSitePlusiQ96T58.
SwissPalmiQ96T58.

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

BgeeiENSG00000065526.
CleanExiHS_SPEN.
ExpressionAtlasiQ96T58. baseline and differential.
GenevisibleiQ96T58. HS.

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
RBPJQ063302EBI-765739,EBI-632552

GO - Molecular functioni

  • RNA polymerase II transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi116655. 44 interactors.
DIPiDIP-34569N.
IntActiQ96T58. 24 interactors.
STRINGi9606.ENSP00000364912.

Structurei

Secondary structure

13664
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi336 – 340Combined sources5
Helixi348 – 359Combined sources12
Helixi360 – 362Combined sources3
Beta strandi365 – 371Combined sources7
Turni374 – 376Combined sources3
Beta strandi378 – 385Combined sources8
Helixi386 – 395Combined sources10
Turni396 – 398Combined sources3
Beta strandi407 – 410Combined sources4
Helixi414 – 422Combined sources9
Beta strandi438 – 444Combined sources7
Helixi451 – 458Combined sources8
Beta strandi464 – 472Combined sources9
Beta strandi475 – 485Combined sources11
Helixi486 – 496Combined sources11
Beta strandi507 – 510Combined sources4
Beta strandi517 – 522Combined sources6
Helixi530 – 537Combined sources8
Helixi538 – 540Combined sources3
Beta strandi543 – 549Combined sources7
Turni550 – 553Combined sources4
Beta strandi554 – 560Combined sources7
Helixi562 – 572Combined sources11
Beta strandi575 – 577Combined sources3
Beta strandi583 – 586Combined sources4
Helixi589 – 601Combined sources13
Helixi609 – 618Combined sources10
Helixi3501 – 3504Combined sources4
Beta strandi3507 – 3515Combined sources9
Beta strandi3518 – 3529Combined sources12
Helixi3531 – 3537Combined sources7
Beta strandi3541 – 3543Combined sources3
Beta strandi3547 – 3549Combined sources3
Beta strandi3551 – 3554Combined sources4
Helixi3557 – 3566Combined sources10
Turni3570 – 3572Combined sources3
Beta strandi3573 – 3580Combined sources8
Helixi3585 – 3598Combined sources14
Helixi3600 – 3606Combined sources7
Beta strandi3608 – 3614Combined sources7
Turni3617 – 3619Combined sources3
Beta strandi3624 – 3629Combined sources6
Helixi3633 – 3642Combined sources10
Helixi3644 – 3650Combined sources7
Turni3651 – 3653Combined sources3
Beta strandi3657 – 3663Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OW1X-ray1.80A3470-3664[»]
2RT5NMR-A3496-3664[»]
4P6QX-ray2.00A335-620[»]
ProteinModelPortaliQ96T58.
SMRiQ96T58.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96T58.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 81RRM 1PROSITE-ProRule annotationAdd BLAST76
Domaini335 – 415RRM 2PROSITE-ProRule annotationAdd BLAST81
Domaini438 – 513RRM 3PROSITE-ProRule annotationAdd BLAST76
Domaini517 – 589RRM 4PROSITE-ProRule annotationAdd BLAST73
Domaini2201 – 2707RIDAdd BLAST507
Domaini3498 – 3664SPOCPROSITE-ProRule annotationAdd BLAST167

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2130 – 2464Interaction with MSX2By similarityAdd BLAST335
Regioni2709 – 2870Interaction with RBPSUHBy similarityAdd BLAST162

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili688 – 715Sequence analysisAdd BLAST28
Coiled coili977 – 1004Sequence analysisAdd BLAST28
Coiled coili1170 – 1191Sequence analysisAdd BLAST22
Coiled coili1408 – 1428Sequence analysisAdd BLAST21
Coiled coili1496 – 1529Sequence analysisAdd BLAST34
Coiled coili1592 – 1612Sequence analysisAdd BLAST21
Coiled coili1928 – 1944Sequence analysisAdd BLAST17

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi125 – 277Arg-richAdd BLAST153
Compositional biasi240 – 325Ser-richAdd BLAST86
Compositional biasi616 – 810Arg-richAdd BLAST195
Compositional biasi624 – 697Tyr-richAdd BLAST74
Compositional biasi2428 – 2520Pro-richAdd BLAST93
Compositional biasi3220 – 3482Pro-richAdd BLAST263

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

eggNOGiKOG0112. Eukaryota.
ENOG410XSAC. LUCA.
GeneTreeiENSGT00530000063730.
HOGENOMiHOG000231295.
HOVERGENiHBG045583.
InParanoidiQ96T58.
OMAiEEEVHYH.
OrthoDBiEOG091G00NR.
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.
IPR016194. SPOC-like_C_dom.
IPR012921. SPOC_C.
IPR010912. SPOC_met.
[Graphical view]
PfamiPF00076. RRM_1. 4 hits.
PF07744. SPOC. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 4 hits.
[Graphical view]
SUPFAMiSSF100939. SSF100939. 1 hit.
SSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 4 hits.
PS50917. SPOC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96T58-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRETRHLWV GNLPENVREE KIIEHFKRYG RVESVKILPK RGSEGGVAAF
60 70 80 90 100
VDFVDIKSAQ KAHNSVNKMG DRDLRTDYNE PGTIPSAARG LDDTVSIASR
110 120 130 140 150
SREVSGFRGG GGGPAYGPPP SLHAREGRYE RRLDGASDNR ERAYEHSAYG
160 170 180 190 200
HHERGTGGFD RTRHYDQDYY RDPRERTLQH GLYYASRSRS PNRFDAHDPR
210 220 230 240 250
YEPRAREQFT LPSVVHRDIY RDDITREVRG RRPERNYQHS RSRSPHSSQS
260 270 280 290 300
RNQSPQRLAS QASRPTRSPS GSGSRSRSSS SDSISSSSST SSDSSDSSSS
310 320 330 340 350
SSDDSPARSV QSAAVPAPTS QLLSSLEKDE PRKSFGIKVQ NLPVRSTDTS
360 370 380 390 400
LKDGLFHEFK KFGKVTSVQI HGTSEERYGL VFFRQQEDQE KALTASKGKL
410 420 430 440 450
FFGMQIEVTA WIGPETESEN EFRPLDERID EFHPKATRTL FIGNLEKTTT
460 470 480 490 500
YHDLRNIFQR FGEIVDIDIK KVNGVPQYAF LQYCDIASVC KAIKKMDGEY
510 520 530 540 550
LGNNRLKLGF GKSMPTNCVW LDGLSSNVSD QYLTRHFCRY GPVVKVVFDR
560 570 580 590 600
LKGMALVLYN EIEYAQAAVK ETKGRKIGGN KIKVDFANRE SQLAFYHCME
610 620 630 640 650
KSGQDIRDFY EMLAERREER RASYDYNQDR TYYESVRTPG TYPEDSRRDY
660 670 680 690 700
PARGREFYSE WETYQGDYYE SRYYDDPREY RDYRNDPYEQ DIREYSYRQR
710 720 730 740 750
ERERERERFE SDRDRDHERR PIERSQSPVH LRRPQSPGAS PSQAERLPSD
760 770 780 790 800
SERRLYSRSS DRSGSCSSLS PPRYEKLDKS RLERYTKNEK TDKERTFDPE
810 820 830 840 850
RVERERRLIR KEKVEKDKTD KQKRKGKVHS PSSQSSETDQ ENEREQSPEK
860 870 880 890 900
PRSCNKLSRE KADKEGIAKN RLELMPCVVL TRVKEKEGKV IDHTPVEKLK
910 920 930 940 950
AKLDNDTVKS SALDQKLQVS QTEPAKSDLS KLESVRMKVP KEKGLSSHVE
960 970 980 990 1000
VVEKEGRLKA RKHLKPEQPA DGVSAVDLEK LEARKRRFAD SNLKAEKQKP
1010 1020 1030 1040 1050
EVKKSSPEME DARVLSKKQP DVSSREVILL REGEAERKPV RKEILKRESK
1060 1070 1080 1090 1100
KIKLDRLNTV ASPKDCQELA SISVGSGSRP SSDLQARLGE LAGESVENQE
1110 1120 1130 1140 1150
VQSKKPIPSK PQLKQLQVLD DQGPEREDVR KNYCSLRDET PERKSGQEKS
1160 1170 1180 1190 1200
HSVNTEEKIG IDIDHTQSYR KQMEQSRRKQ QMEMEIAKSE KFGSPKKDVD
1210 1220 1230 1240 1250
EYERRSLVHE VGKPPQDVTD DSPPSKKKRM DHVDFDICTK RERNYRSSRQ
1260 1270 1280 1290 1300
ISEDSERTGG SPSVRHGSFH EDEDPIGSPR LLSVKGSPKV DEKVLPYSNI
1310 1320 1330 1340 1350
TVREESLKFN PYDSSRREQM ADMAKIKLSV LNSEDELNRW DSQMKQDAGR
1360 1370 1380 1390 1400
FDVSFPNSII KRDSLRKRSV RDLEPGEVPS DSDEDGEHKS HSPRASALYE
1410 1420 1430 1440 1450
SSRLSFLLRD REDKLRERDE RLSSSLERNK FYSFALDKTI TPDTKALLER
1460 1470 1480 1490 1500
AKSLSSSREE NWSFLDWDSR FANFRNNKDK EKVDSAPRPI PSWYMKKKKI
1510 1520 1530 1540 1550
RTDSEGKMDD KKEDHKEEEQ ERQELFASRF LHSSIFEQDS KRLQHLERKE
1560 1570 1580 1590 1600
EDSDFISGRI YGKQTSEGAN STTDSIQEPV VLFHSRFMEL TRMQQKEKEK
1610 1620 1630 1640 1650
DQKPKEVEKQ EDTENHPKTP ESAPENKDSE LKTPPSVGPP SVTVVTLESA
1660 1670 1680 1690 1700
PSALEKTTGD KTVEAPLVTE EKTVEPATVS EEAKPASEPA PAPVEQLEQV
1710 1720 1730 1740 1750
DLPPGADPDK EAAMMPAGVE EGSSGDQPPY LDAKPPTPGA SFSQAESNVD
1760 1770 1780 1790 1800
PEPDSTQPLS KPAQKSEEAN EPKAEKPDAT ADAEPDANQK AEAAPESQPP
1810 1820 1830 1840 1850
ASEDLEVDPP VAAKDKKPNK SKRSKTPVQA AAVSIVEKPV TRKSERIDRE
1860 1870 1880 1890 1900
KLKRSNSPRG EAQKLLELKM EAEKITRTAS KNSAADLEHP EPSLPLSRTR
1910 1920 1930 1940 1950
RRNVRSVYAT MGDHENRSPV KEPVEQPRVT RKRLERELQE AAAVPTTPRR
1960 1970 1980 1990 2000
GRPPKTRRRA DEEEENEAKE PAETLKPPEG WRSPRSQKTA AGGGPQGKKG
2010 2020 2030 2040 2050
KNEPKVDATR PEATTEVGPQ IGVKESSMEP KAAEEEAGSE QKRDRKDAGT
2060 2070 2080 2090 2100
DKNPPETAPV EVVEKKPAPE KNSKSKRGRS RNSRLAVDKS ASLKNVDAAV
2110 2120 2130 2140 2150
SPRGAAAQAG ERESGVVAVS PEKSESPQKE DGLSSQLKSD PVDPDKEPEK
2160 2170 2180 2190 2200
EDVSASGPSP EATQLAKQME LEQAVEHIAK LAEASASAAY KADAPEGLAP
2210 2220 2230 2240 2250
EDRDKPAHQA SETELAAAIG SIINDISGEP ENFPAPPPYP GESQTDLQPP
2260 2270 2280 2290 2300
AGAQALQPSE EGMETDEAVS GILETEAATE SSRPPVNAPD PSAGPTDTKE
2310 2320 2330 2340 2350
ARGNSSETSH SVPEAKGSKE VEVTLVRKDK GRQKTTRSRR KRNTNKKVVA
2360 2370 2380 2390 2400
PVESHVPESN QAQGESPAAN EGTTVQHPEA PQEEKQSEKP HSTPPQSCTS
2410 2420 2430 2440 2450
DLSKIPSTEN SSQEISVEER TPTKASVPPD LPPPPQPAPV DEEPQARFRV
2460 2470 2480 2490 2500
HSIIESDPVT PPSDPSIPIP TLPSVTAAKL SPPVASGGIP HQSPPTKVTE
2510 2520 2530 2540 2550
WITRQEEPRA QSTPSPALPP DTKASDVDTS SSTLRKILMD PKYVSATSVT
2560 2570 2580 2590 2600
STSVTTAIAE PVSAAPCLHE APPPPVDSKK PLEEKTAPPV TNNSEIQASE
2610 2620 2630 2640 2650
VLVAADKEKV APVIAPKITS VISRMPVSID LENSQKITLA KPAPQTLTGL
2660 2670 2680 2690 2700
VSALTGLVNV SLVPVNALKG PVKGSVTTLK SLVSTPAGPV NVLKGPVNVL
2710 2720 2730 2740 2750
TGPVNVLTTP VNATVGTVNA APGTVNAAAS AVNATASAVT VTAGAVTAAS
2760 2770 2780 2790 2800
GGVTATTGTV TMAGAVIAPS TKCKQRASAN ENSRFHPGSM PVIDDRPADA
2810 2820 2830 2840 2850
GSGAGLRVNT SEGVVLLSYS GQKTEGPQRI SAKISQIPPA SAMDIEFQQS
2860 2870 2880 2890 2900
VSKSQVKPDS VTASQPPSKG PQAPAGYANV ATHSTLVLTA QTYNASPVIS
2910 2920 2930 2940 2950
SVKADRPSLE KPEPIHLSVS TPVTQGGTVK VLTQGINTPP VLVHNQLVLT
2960 2970 2980 2990 3000
PSIVTTNKKL ADPVTLKIET KVLQPANLGS TLTPHHPPAL PSKLPTEVNH
3010 3020 3030 3040 3050
VPSGPSIPAD RTVSHLAAAK LDAHSPRPSG PGPSSFPRAS HPSSTASTAL
3060 3070 3080 3090 3100
STNATVMLAA GIPVPQFISS IHPEQSVIMP PHSITQTVSL SHLSQGEVRM
3110 3120 3130 3140 3150
NTPTLPSITY SIRPEALHSP RAPLQPQQIE VRAPQRASTP QPAPAGVPAL
3160 3170 3180 3190 3200
ASQHPPEEEV HYHLPVARAT APVQSEVLVM QSEYRLHPYT VPRDVRIMVH
3210 3220 3230 3240 3250
PHVTAVSEQP RAADGVVKVP PASKAPQQPG KEAAKTPDAK AAPTPTPAPV
3260 3270 3280 3290 3300
PVPVPLPAPA PAPHGEARIL TVTPSNQLQG LPLTPPVVVT HGVQIVHSSG
3310 3320 3330 3340 3350
ELFQEYRYGD IRTYHPPAQL THTQFPAASS VGLPSRTKTA AQGPPPEGEP
3360 3370 3380 3390 3400
LQPPQPVQST QPAQPAPPCP PSQLGQPGQP PSSKMPQVSQ EAKGTQTGVE
3410 3420 3430 3440 3450
QPRLPAGPAN RPPEPHTQVQ RAQAETGPTS FPSPVSVSMK PDLPVSLPTQ
3460 3470 3480 3490 3500
TAPKQPLFVP TTSGPSTPPG LVLPHTEFQP APKQDSSPHL TSQRPVDMVQ
3510 3520 3530 3540 3550
LLKKYPIVWQ GLLALKNDTA AVQLHFVSGN NVLAHRSLPL SEGGPPLRIA
3560 3570 3580 3590 3600
QRMRLEATQL EGVARRMTVE TDYCLLLALP CGRDQEDVVS QTESLKAAFI
3610 3620 3630 3640 3650
TYLQAKQAAG IINVPNPGSN QPAYVLQIFP PCEFSESHLS RLAPDLLASI
3660
SNISPHLMIV IASV
Length:3,664
Mass (Da):402,248
Last modified:December 1, 2001 - v1
Checksum:i5228C58533E5B27B
GO

Sequence cautioni

The sequence BAA91405 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14324 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB51072 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti956G → D (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017119970A → V.Corresponds to variant rs848208dbSNPEnsembl.1
Natural variantiVAR_035483990D → H in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0171201091L → P.1 PublicationCorresponds to variant rs848209dbSNPEnsembl.1
Natural variantiVAR_0522081363D → E.Corresponds to variant rs12095818dbSNPEnsembl.1
Natural variantiVAR_0354841488R → I in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0171212360N → D.Corresponds to variant rs848210dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OW1X-ray1.80A3470-3664[»]
2RT5NMR-A3496-3664[»]
4P6QX-ray2.00A335-620[»]
ProteinModelPortaliQ96T58.
SMRiQ96T58.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116655. 44 interactors.
DIPiDIP-34569N.
IntActiQ96T58. 24 interactors.
STRINGi9606.ENSP00000364912.

PTM databases

iPTMnetiQ96T58.
PhosphoSitePlusiQ96T58.
SwissPalmiQ96T58.

Polymorphism and mutation databases

BioMutaiSPEN.
DMDMi41688816.

Proteomic databases

EPDiQ96T58.
MaxQBiQ96T58.
PaxDbiQ96T58.
PeptideAtlasiQ96T58.
PRIDEiQ96T58.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375759; ENSP00000364912; ENSG00000065526.
GeneIDi23013.
KEGGihsa:23013.
UCSCiuc001axk.2. human.

Organism-specific databases

CTDi23013.
DisGeNETi23013.
GeneCardsiSPEN.
H-InvDBHIX0159662.
HGNCiHGNC:17575. SPEN.
HPAiHPA015825.
HPA050257.
MIMi613484. gene.
neXtProtiNX_Q96T58.
OpenTargetsiENSG00000065526.
PharmGKBiPA134895302.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0112. Eukaryota.
ENOG410XSAC. LUCA.
GeneTreeiENSGT00530000063730.
HOGENOMiHOG000231295.
HOVERGENiHBG045583.
InParanoidiQ96T58.
OMAiEEEVHYH.
OrthoDBiEOG091G00NR.
PhylomeDBiQ96T58.
TreeFamiTF315637.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000065526-MONOMER.
SIGNORiQ96T58.

Miscellaneous databases

ChiTaRSiSPEN. human.
EvolutionaryTraceiQ96T58.
GeneWikiiSPEN.
GenomeRNAii23013.
PROiQ96T58.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000065526.
CleanExiHS_SPEN.
ExpressionAtlasiQ96T58. baseline and differential.
GenevisibleiQ96T58. HS.

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.
IPR016194. SPOC-like_C_dom.
IPR012921. SPOC_C.
IPR010912. SPOC_met.
[Graphical view]
PfamiPF00076. RRM_1. 4 hits.
PF07744. SPOC. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 4 hits.
[Graphical view]
SUPFAMiSSF100939. SSF100939. 1 hit.
SSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 4 hits.
PS50917. SPOC. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.