Q96T58 (MINT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Msx2-interacting protein

Alternative name(s):
SMART/HDAC1-associated repressor protein
SPEN homolog

Gene names

Name:	SPEN
Synonyms:	KIAA0929, MINT, SHARP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	3664 AA.
Sequence status	Complete.
Protein existence	Evidence 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.15 The SPOC domain, which mediates the interaction with NCOR2, is essential for the repressive activity. Ref.15
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 process	Host-virus interaction Notch signaling pathway Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Activator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of neurogenesis Inferred from mutant phenotype PubMed 16287852. Source: BHF-UCL positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	transcriptional repressor complex Inferred from direct assay PubMed 16287852. Source: BHF-UCL
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW 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 sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara single-stranded DNA binding Inferred from electronic annotation. Source: Compara transcription corepressor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	3	EBI-765739,EBI-389883

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 3664

3664

Msx2-interacting protein

PRO_0000081627

Regions

Domain

6 – 81

76

RRM 1

Domain

335 – 415

81

RRM 2

Domain

438 – 513

76

RRM 3

Domain

517 – 589

73

RRM 4

Domain

2201 – 2707

507

RID

Domain

3498 – 3664

167

SPOC

DNA binding

1 – 573

573

By similarity

Region

2130 – 2464

335

Interaction with MSX2 By similarity

Region

2709 – 2870

162

Interaction with RBPSUH By similarity

Coiled coil

688 – 715

28

Potential

Coiled coil

977 – 1004

28

Potential

Coiled coil

1170 – 1191

22

Potential

Coiled coil

1408 – 1428

21

Potential

Coiled coil

1496 – 1529

34

Potential

Coiled coil

1592 – 1612

21

Potential

Coiled coil

1928 – 1944

17

Potential

Compositional bias

125 – 277

153

Arg-rich

Compositional bias

240 – 325

86

Ser-rich

Compositional bias

616 – 810

195

Arg-rich

Compositional bias

624 – 697

74

Tyr-rich

Compositional bias

2428 – 2520

93

Pro-rich

Compositional bias

3220 – 3482

263

Pro-rich

Amino acid modifications

Modified residue

309

1

Phosphoserine Ref.13

Modified residue

623

1

Phosphoserine Ref.13

Modified residue

727

1

Phosphoserine Ref.13 Ref.14

Modified residue

736

1

Phosphoserine Ref.11

Modified residue

740

1

Phosphoserine Ref.11

Modified residue

1062

1

Phosphoserine Ref.14

Modified residue

1194

1

Phosphoserine Ref.11

Modified residue

1222

1

Phosphoserine Ref.12 Ref.14

Modified residue

1252

1

Phosphoserine Ref.13

Modified residue

1261

1

Phosphoserine Ref.14

Modified residue

1268

1

Phosphoserine Ref.9 Ref.12 Ref.13 Ref.14

Modified residue

1278

1

Phosphoserine Ref.9 Ref.12 Ref.13 Ref.14

Modified residue

1283

1

Phosphoserine Ref.9

Modified residue

1287

1

Phosphoserine Ref.11 Ref.13

Modified residue

1333

1

Phosphoserine Ref.13

Modified residue

1380

1

Phosphoserine Ref.9 Ref.11 Ref.14

Modified residue

1382

1

Phosphoserine Ref.9 Ref.11 Ref.14

Modified residue

1439

1

Phosphothreonine Ref.11

Modified residue

1441

1

Phosphothreonine Ref.11

Modified residue

1633

1

Phosphothreonine Ref.13

Modified residue

1897

1

Phosphoserine Ref.11 Ref.13

Modified residue

1947

1

Phosphothreonine Ref.12

Modified residue

2101

1

Phosphoserine Ref.13 Ref.14

Modified residue

2120

1

Phosphoserine Ref.11 Ref.13 Ref.14

Modified residue

2126

1

Phosphoserine Ref.11

Modified residue

2159

1

Phosphoserine Ref.13

Modified residue

2366

1

Phosphoserine Ref.11

Modified residue

2421

1

Phosphothreonine Ref.11

Modified residue

2452

1

Phosphoserine Ref.12

Modified residue

2460

1

Phosphothreonine Ref.12

Modified residue

2938

1

Phosphothreonine Ref.11

Modified residue

2950

1

Phosphothreonine Ref.11

Modified residue

3433

1

Phosphoserine Ref.11

Natural variations

Natural variant

970

1

A → V.
Corresponds to variant rs848208 [ dbSNP | Ensembl ].

VAR_017119

Natural variant

990

1

D → H in a breast cancer sample; somatic mutation. Ref.16

VAR_035483

Natural variant

1091

1

L → P. Ref.4
Corresponds to variant rs848209 [ dbSNP | Ensembl ].

VAR_017120

Natural variant

1363

1

D → E.
Corresponds to variant rs12095818 [ dbSNP | Ensembl ].

VAR_052208

Natural variant

1488

1

R → I in a breast cancer sample; somatic mutation. Ref.16

VAR_035484

Natural variant

2360

1

N → D.
Corresponds to variant rs848210 [ dbSNP | Ensembl ].

VAR_017121

Experimental info

Sequence conflict

956

1

G → D Ref.4

Secondary structure

1

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3664

Helix Strand Turn

Details...

Helix

3501 – 3504

4

Beta strand

3507 – 3515

9

Beta strand

3518 – 3529

12

Helix

3531 – 3537

7

Beta strand

3547 – 3549

3

Beta strand

3551 – 3554

4

Helix

3557 – 3566

10

Turn

3570 – 3572

3

Beta strand

3573 – 3580

8

Helix

3585 – 3598

14

Helix

3600 – 3606

7

Beta strand

3608 – 3614

7

Beta strand

3624 – 3629

6

Helix

3633 – 3642

10

Helix

3644 – 3650

7

Turn

3651 – 3653

3

Beta strand

3657 – 3663

7

Sequences

	Sequence		Length	Mass (Da)
	Q96T58 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 5228C58533E5B27B	FASTA	3,664	402,248
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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, MASS SPECTROMETRY.
[15]	"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.
[16]	"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. , 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.

IPI

IPI00045914.

RefSeq

NP_055816.2. NM_015001.2.

UniGene

Hs.731396.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OW1	X-ray	1.80	A	3470-3664	[»]

ProteinModelPortal

Q96T58.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96T58. 19 interactions.

STRING

9606.ENSP00000364912.

PTM databases

PhosphoSite

Q96T58.

Polymorphism databases

DMDM

41688816.

Proteomic databases

PaxDb

Q96T58.

PRIDE

Q96T58.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375759; ENSP00000364912; ENSG00000065526.

GeneID

23013.

KEGG

hsa:23013.

UCSC

uc001axk.1. human.

Organism-specific databases

CTD

23013.

GeneCards

GC01P016174.

H-InvDB

HIX0159662.

HGNC

HGNC:17575. SPEN.

HPA

HPA015825.

MIM

613484. gene.

neXtProt

NX_Q96T58.

PharmGKB

PA134895302.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOGENOM

HOG000231295.

HOVERGEN

HBG045583.

InParanoid

Q96T58.

OMA

KHLKPEQ.

OrthoDB

EOG4JM7NS.

PhylomeDB

Q96T58.

Gene expression databases

ArrayExpress

Q96T58.

Bgee

Q96T58.

CleanEx

HS_SPEN.

Genevestigator

Q96T58.

GermOnline

ENSG00000065526. Homo sapiens.

Family and domain databases

Gene3D

2.40.290.10. 1 hit.
3.30.70.330. 4 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR012921. SPOC_C.
IPR016194. SPOC_like_C_dom.
IPR010912. SPOC_met.
[Graphical view]

Pfam

PF00076. RRM_1. 3 hits.
PF07744. SPOC. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 4 hits.
[Graphical view]

SUPFAM

SSF100939. SPOC-like. 1 hit.

PROSITE

PS50102. RRM. 4 hits.
PS50917. SPOC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SPEN. human.

EvolutionaryTrace

Q96T58.

GenomeRNAi

23013.

NextBio

43936.

SOURCE

Search...

Entry information

Entry name

MINT_HUMAN

Accession

Primary (citable) accession number: Q96T58
Secondary accession number(s): Q9H9A8 , Q9NWH5, Q9UQ01, Q9Y556

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.