Reviewed, UniProtKB/Swiss-Prot Q02447 (SP3_HUMAN)

Names and origin

Protein names

Recommended name:
    Transcription factor Sp3
Alternative name(s):
    SPR-2

Gene names

Name:

SP3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	781 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone-induction and house-keeping. Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Subunit structure	Interacts with HLTF; the interaction may be required for basal transcriptional activity of HLTF. Interacts with HDAC1; the interaction deacetylates SP3 and regulates its transcriptional activity. Interacts with HDAC2 (preferably the CK2-phosphorylated form); the interaction deacetylates SP3 and regulates its transcriptional activity. Ref.11 Ref.15 Ref.13
Subcellular location	Nucleus. Note: Localizes to the nuclear periphery and in nuclear dots when sumoylated. Some localization in PML nuclear bodies. Ref.14 Ref.17 Ref.20
Tissue specificity	Ubiquitously expressed.
Post-translational modification	Not glycosylated. Ref.16 Acetylated by histone acetyltransferase p300, deacetylated by HDACs. Acetylation/deacetylation states regulate transcriptional activity. Acetylation appears to activate transcription. Alternate sumoylation and acetylation at Lys-551 also control transcriptional activity. Sumoylated on all isoforms. Sumoylated on 2 sites in longer isoforms with Lys-551 being the major site. Sumoylation at this site promotes nuclear localization to the nuclear periphery, nuclear dots and PML nuclear bodies. Sumoylation on Lys-551 represses the transactivation activity, except for the largest isoform, L-Sp3, which has little effect on transactivation. Alternate sumoylation and acetylation at Lys-551 also control transcriptional activity. Ref.14 Ref.16 Ref.17 Ref.19 Ref.21
Sequence similarities	Belongs to the Sp1 C2H2-type zinc-finger protein family. Contains 3 C2H2-type zinc fingers.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative initiation Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred by curator. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct transcription activator activity Ref.10 Inferred from direct assay. Source: UniProtKB transcription repressor activity Ref.10 Non-traceable author statement. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GCH1	P30793	2	EBI-348158,EBI-958183
STK19	P49842	1	EBI-348158,EBI-347581

Alternative products

This entry describes 6 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Isoform 1 (identifier: Q02447-1)

Also known as: Large; L-Sp3;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q02447-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.

Note: Produced by alternative initiation at Met-13 of isoform 1. No experimental confirmation available.

Isoform 3 (identifier: Q02447-3)

Also known as: M1-Sp3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-285: Missing.

Note: Produced by alternative initiation at Met-286 of isoform 1. No experimental confirmation available.

Isoform 4 (identifier: Q02447-4)

Also known as: M2-Sp3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-302: Missing.

Note: Produced by alternative initiation at Met-303 of isoform 1. No experimental confirmation available.

Isoform 5 (identifier: Q02447-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.
     69-69: I → M

Note: Produced by alternative splicing. An AUA codon is translated into Met and used as a translation initiation site (in vitro).

Isoform 6 (identifier: Q02447-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.
     53-93: Missing.

Note: Produced by alternative splicing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 781	781	Transcription factor Sp3		PRO_0000047141
Regions
	Zinc finger	621 – 645	25	C2H2-type 1
	Zinc finger	651 – 675	25	C2H2-type 2
	Zinc finger	681 – 703	23	C2H2-type 3
	Region	138 – 237	100	Transactivation domain (Gln-rich)
	Region	350 – 499	150	Transactivation domain (Gln-rich)
	Region	534 – 620	87	Repressor domain
	Compositional bias	21 – 31	11	Poly-Gly
	Compositional bias	35 – 39	5	Poly-Gln
	Compositional bias	44 – 100	57	Ala-rich
Amino acid modifications
	Modified residue	73	1	Phosphoserine Ref.22
	Modified residue	551	1	N6-acetyllysine; alternate Ref.12 Ref.18
	Modified residue	563	1	Phosphoserine Ref.22
	Modified residue	566	1	Phosphoserine Ref.22
	Modified residue	646	1	Phosphoserine Ref.22
	Cross-link	120		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.14
	Cross-link	551		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.14 Ref.17 Ref.19 Ref.21
Natural variations
	Alternative sequence	1 – 302	302	Missing in isoform 4.		VSP_026698
	Alternative sequence	1 – 285	285	Missing in isoform 3.		VSP_026699
	Alternative sequence	1 – 68	68	Missing in isoform 5.		VSP_026700
	Alternative sequence	1 – 12	12	Missing in isoform 2 and isoform 6.		VSP_026701
	Alternative sequence	53 – 93	41	Missing in isoform 6.		VSP_026702
	Alternative sequence	69	1	I → M in isoform 5.		VSP_026703
	Natural variant	164	1	T → A: dbSNP rs1047640. Ref.1 Ref.2 Ref.9		VAR_016123
Experimental info
	Mutagenesis	120	1	K → R: Some loss of sumoylation. Slight increase in transcriptional activity. Large increase in transcriptional activity; when associated with R-551. Ref.14
	Mutagenesis	551 – 553	3	KEE → AAA: Increases transcriptional activity. Ref.14 Ref.17 Ref.19
	Mutagenesis	551 – 553	3	KEE → REA: 200-fold increase in transcriptional activation. Ref.14 Ref.17 Ref.19
	Mutagenesis	551 – 553	3	KEE → RED: 200-fold increase in transcriptional activation. Ref.14 Ref.17 Ref.19
	Mutagenesis	551 – 552	2	KE → RA: 200-fold increase in transcriptional activation. Ref.14 Ref.19
	Mutagenesis	551 – 552	2	KE → RD: 200-fold increase in transcriptional activation. Ref.14 Ref.19
	Mutagenesis	551	1	K → R: Great loss of sumoylation, 20-fold increase in transcriptional activity and diffuse nuclear localization. Further small increase in transcriptional activity; when associated with R-120. Ref.14 Ref.19
	Sequence conflict	69	1	I → M in AAR30505. Ref.2
	Sequence conflict	71	1	P → G in AAA36630. Ref.7
	Sequence conflict	739	1	N → K in AAL58086. Ref.1
	Sequence conflict	739	1	N → K in AAR30505. Ref.2
	Sequence conflict	739	1	N → K in AAR30506. Ref.2
	Sequence conflict	739	1	N → K in CAA48562. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Large) (L-Sp3) [UniParc]. Last modified May 16, 2003. Version 3. Checksum: DCFD4363509DB49D	FASTA	781	81,925
	10 20 30 40 50 60 MTAPEKPVKQ EEMAALDVDS GGGGGGGGGH GEYLQQQQQH GNGAVAAAAA AQDTQPSPLA 70 80 90 100 110 120 LLAATCSKIG PPSPGDDEEE AAAAAGAPAA AGATGDLASA QLGGAPNRWE VLSATPTTIK 130 140 150 160 170 180 DEAGNLVQIP SAATSSGQYV LPLQNLQNQQ IFSVAPGSDS SNGTVSSVQY QVIPQIQSAD 190 200 210 220 230 240 GQQVQIGFTG SSDNGGINQE SSQIQIIPGS NQTLLASGTP SANIQNLIPQ TGQVQVQGVA 250 260 270 280 290 300 IGGSSFPGQT QVVANVPLGL PGNITFVPIN SVDLDSLGLS GSSQTMTAGI NADGHLINTG 310 320 330 340 350 360 QAMDSSDNSE RTGERVSPDI NETNTDTDLF VPTSSSSQLP VTIDSTGILQ QNTNSLTTSS 370 380 390 400 410 420 GQVHSSDLQG NYIQSPVSEE TQAQNIQVST AQPVVQHLQL QESQQPTSQA QIVQGITPQT 430 440 450 460 470 480 IHGVQASGQN ISQQALQNLQ LQLNPGTFLI QAQTVTPSGQ VTWQTFQVQG VQNLQNLQIQ 490 500 510 520 530 540 NTAAQQITLT PVQTLTLGQV AAGGAFTSTP VSLSTGQLPN LQTVTVNSID SAGIQLHPGE 550 560 570 580 590 600 NADSPADIRI KEEEPDPEEW QLSGDSTLNT NDLTHLRVQV VDEEGDQQHQ EGKRLRRVAC 610 620 630 640 650 660 TCPNCKEGGG RGTNLGKKKQ HICHIPGCGK VYGKTSHLRA HLRWHSGERP FVCNWMYCGK 670 680 690 700 710 720 RFTRSDELQR HRRTHTGEKK FVCPECSKRF MRSDHLAKHI KTHQNKKGIH SSSTVLASVE 730 740 750 760 770 780 AARDDTLITA GGTTLILANI QQGSVSGIGT VNTSATSNQD ILTNTEIPLQ LVTVSGNETM E
	Isoform 2. Checksum: C02D0B852BBF9389	FASTA	769	80,557
	10 20 30 40 50 60 MAALDVDSGG GGGGGGGHGE YLQQQQQHGN GAVAAAAAAQ DTQPSPLALL AATCSKIGPP 70 80 90 100 110 120 SPGDDEEEAA AAAGAPAAAG ATGDLASAQL GGAPNRWEVL SATPTTIKDE AGNLVQIPSA 130 140 150 160 170 180 ATSSGQYVLP LQNLQNQQIF SVAPGSDSSN GTVSSVQYQV IPQIQSADGQ QVQIGFTGSS 190 200 210 220 230 240 DNGGINQESS QIQIIPGSNQ TLLASGTPSA NIQNLIPQTG QVQVQGVAIG GSSFPGQTQV 250 260 270 280 290 300 VANVPLGLPG NITFVPINSV DLDSLGLSGS SQTMTAGINA DGHLINTGQA MDSSDNSERT 310 320 330 340 350 360 GERVSPDINE TNTDTDLFVP TSSSSQLPVT IDSTGILQQN TNSLTTSSGQ VHSSDLQGNY 370 380 390 400 410 420 IQSPVSEETQ AQNIQVSTAQ PVVQHLQLQE SQQPTSQAQI VQGITPQTIH GVQASGQNIS 430 440 450 460 470 480 QQALQNLQLQ LNPGTFLIQA QTVTPSGQVT WQTFQVQGVQ NLQNLQIQNT AAQQITLTPV 490 500 510 520 530 540 QTLTLGQVAA GGAFTSTPVS LSTGQLPNLQ TVTVNSIDSA GIQLHPGENA DSPADIRIKE 550 560 570 580 590 600 EEPDPEEWQL SGDSTLNTND LTHLRVQVVD EEGDQQHQEG KRLRRVACTC PNCKEGGGRG 610 620 630 640 650 660 TNLGKKKQHI CHIPGCGKVY GKTSHLRAHL RWHSGERPFV CNWMYCGKRF TRSDELQRHR 670 680 690 700 710 720 RTHTGEKKFV CPECSKRFMR SDHLAKHIKT HQNKKGIHSS STVLASVEAA RDDTLITAGG 730 740 750 760 TTLILANIQQ GSVSGIGTVN TSATSNQDIL TNTEIPLQLV TVSGNETME
	Isoform 3 (M1-Sp3). Checksum: 65658E7F04158661	FASTA	496	53,715
	10 20 30 40 50 60 MTAGINADGH LINTGQAMDS SDNSERTGER VSPDINETNT DTDLFVPTSS SSQLPVTIDS 70 80 90 100 110 120 TGILQQNTNS LTTSSGQVHS SDLQGNYIQS PVSEETQAQN IQVSTAQPVV QHLQLQESQQ 130 140 150 160 170 180 PTSQAQIVQG ITPQTIHGVQ ASGQNISQQA LQNLQLQLNP GTFLIQAQTV TPSGQVTWQT 190 200 210 220 230 240 FQVQGVQNLQ NLQIQNTAAQ QITLTPVQTL TLGQVAAGGA FTSTPVSLST GQLPNLQTVT 250 260 270 280 290 300 VNSIDSAGIQ LHPGENADSP ADIRIKEEEP DPEEWQLSGD STLNTNDLTH LRVQVVDEEG 310 320 330 340 350 360 DQQHQEGKRL RRVACTCPNC KEGGGRGTNL GKKKQHICHI PGCGKVYGKT SHLRAHLRWH 370 380 390 400 410 420 SGERPFVCNW MYCGKRFTRS DELQRHRRTH TGEKKFVCPE CSKRFMRSDH LAKHIKTHQN 430 440 450 460 470 480 KKGIHSSSTV LASVEAARDD TLITAGGTTL ILANIQQGSV SGIGTVNTSA TSNQDILTNT 490 EIPLQLVTVS GNETME
	Isoform 4 (M2-Sp3). Checksum: DA04C2A90DFA307A	FASTA	479	52,050
	10 20 30 40 50 60 MDSSDNSERT GERVSPDINE TNTDTDLFVP TSSSSQLPVT IDSTGILQQN TNSLTTSSGQ 70 80 90 100 110 120 VHSSDLQGNY IQSPVSEETQ AQNIQVSTAQ PVVQHLQLQE SQQPTSQAQI VQGITPQTIH 130 140 150 160 170 180 GVQASGQNIS QQALQNLQLQ LNPGTFLIQA QTVTPSGQVT WQTFQVQGVQ NLQNLQIQNT 190 200 210 220 230 240 AAQQITLTPV QTLTLGQVAA GGAFTSTPVS LSTGQLPNLQ TVTVNSIDSA GIQLHPGENA 250 260 270 280 290 300 DSPADIRIKE EEPDPEEWQL SGDSTLNTND LTHLRVQVVD EEGDQQHQEG KRLRRVACTC 310 320 330 340 350 360 PNCKEGGGRG TNLGKKKQHI CHIPGCGKVY GKTSHLRAHL RWHSGERPFV CNWMYCGKRF 370 380 390 400 410 420 TRSDELQRHR RTHTGEKKFV CPECSKRFMR SDHLAKHIKT HQNKKGIHSS STVLASVEAA 430 440 450 460 470 RDDTLITAGG TTLILANIQQ GSVSGIGTVN TSATSNQDIL TNTEIPLQLV TVSGNETME
	Isoform 5. Checksum: B0CF8FC66DA30478	FASTA	713	75,330
	10 20 30 40 50 60 MGPPSPGDDE EEAAAAAGAP AAAGATGDLA SAQLGGAPNR WEVLSATPTT IKDEAGNLVQ 70 80 90 100 110 120 IPSAATSSGQ YVLPLQNLQN QQIFSVAPGS DSSNGTVSSV QYQVIPQIQS ADGQQVQIGF 130 140 150 160 170 180 TGSSDNGGIN QESSQIQIIP GSNQTLLASG TPSANIQNLI PQTGQVQVQG VAIGGSSFPG 190 200 210 220 230 240 QTQVVANVPL GLPGNITFVP INSVDLDSLG LSGSSQTMTA GINADGHLIN TGQAMDSSDN 250 260 270 280 290 300 SERTGERVSP DINETNTDTD LFVPTSSSSQ LPVTIDSTGI LQQNTNSLTT SSGQVHSSDL 310 320 330 340 350 360 QGNYIQSPVS EETQAQNIQV STAQPVVQHL QLQESQQPTS QAQIVQGITP QTIHGVQASG 370 380 390 400 410 420 QNISQQALQN LQLQLNPGTF LIQAQTVTPS GQVTWQTFQV QGVQNLQNLQ IQNTAAQQIT 430 440 450 460 470 480 LTPVQTLTLG QVAAGGAFTS TPVSLSTGQL PNLQTVTVNS IDSAGIQLHP GENADSPADI 490 500 510 520 530 540 RIKEEEPDPE EWQLSGDSTL NTNDLTHLRV QVVDEEGDQQ HQEGKRLRRV ACTCPNCKEG 550 560 570 580 590 600 GGRGTNLGKK KQHICHIPGC GKVYGKTSHL RAHLRWHSGE RPFVCNWMYC GKRFTRSDEL 610 620 630 640 650 660 QRHRRTHTGE KKFVCPECSK RFMRSDHLAK HIKTHQNKKG IHSSSTVLAS VEAARDDTLI 670 680 690 700 710 TAGGTTLILA NIQQGSVSGI GTVNTSATSN QDILTNTEIP LQLVTVSGNE TME
	Isoform 6. Checksum: E9D95D6717E9F885	FASTA	728	76,814
	10 20 30 40 50 60 MAALDVDSGG GGGGGGGHGE YLQQQQQHGN GAVAAAAAAQ TGDLASAQLG GAPNRWEVLS 70 80 90 100 110 120 ATPTTIKDEA GNLVQIPSAA TSSGQYVLPL QNLQNQQIFS VAPGSDSSNG TVSSVQYQVI 130 140 150 160 170 180 PQIQSADGQQ VQIGFTGSSD NGGINQESSQ IQIIPGSNQT LLASGTPSAN IQNLIPQTGQ 190 200 210 220 230 240 VQVQGVAIGG SSFPGQTQVV ANVPLGLPGN ITFVPINSVD LDSLGLSGSS QTMTAGINAD 250 260 270 280 290 300 GHLINTGQAM DSSDNSERTG ERVSPDINET NTDTDLFVPT SSSSQLPVTI DSTGILQQNT 310 320 330 340 350 360 NSLTTSSGQV HSSDLQGNYI QSPVSEETQA QNIQVSTAQP VVQHLQLQES QQPTSQAQIV 370 380 390 400 410 420 QGITPQTIHG VQASGQNISQ QALQNLQLQL NPGTFLIQAQ TVTPSGQVTW QTFQVQGVQN 430 440 450 460 470 480 LQNLQIQNTA AQQITLTPVQ TLTLGQVAAG GAFTSTPVSL STGQLPNLQT VTVNSIDSAG 490 500 510 520 530 540 IQLHPGENAD SPADIRIKEE EPDPEEWQLS GDSTLNTNDL THLRVQVVDE EGDQQHQEGK 550 560 570 580 590 600 RLRRVACTCP NCKEGGGRGT NLGKKKQHIC HIPGCGKVYG KTSHLRAHLR WHSGERPFVC 610 620 630 640 650 660 NWMYCGKRFT RSDELQRHRR THTGEKKFVC PECSKRFMRS DHLAKHIKTH QNKKGIHSSS 670 680 690 700 710 720 TVLASVEAAR DDTLITAGGT TLILANIQQG SVSGIGTVNT SATSNQDILT NTEIPLQLVT VSGNETME

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"AUA as a translation initiation site in vitro for the human transcription factor Sp3." Hernandez E.M., Johnson A., Notario V., Chen A., Richert J.R. J. Biochem. Mol. Biol. 35:273-282(2002) [PubMed: 12297010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANT ALA-164.
[2]	"Human transcription factor Sp3: genomic structure, identification of a processed pseudogene, and transcript analysis." Moran K.M., Crusio R.H., Chan C.H., Grekova M.C., Richert J.R. Gene 341:235-247(2004) [PubMed: 15474306] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), ALTERNATIVE INITIATION (ISOFORMS 2; 3 AND 4), VARIANT ALA-164.
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Trachea.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lung.
[5]	"5' genomic structure of human Sp3." Oleksiak M.F., Crawford D.L. Mol. Biol. Evol. 19:2026-2029(2002) [PubMed: 12411611] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
[6]	"Regulation of hTERT-gene transcription by SP3." Meyer-Grahle U. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-112.
[7]	Kingsley C., Winoto A. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 71-781, SEQUENCE REVISION. Tissue: T-cell.
[8]	"Cloning of GT box-binding proteins: a novel Sp1 multigene family regulating T-cell receptor gene expression." Kingsley C., Winoto A. Mol. Cell. Biol. 12:4251-4261(1992) [PubMed: 1341900] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 129-781.
[9]	"Cloning by recognition site screening of two novel GT box binding proteins: a family of Sp1 related genes." Hagen G., Mueller S., Beato M., Suske G. Nucleic Acids Res. 20:5519-5525(1992) [PubMed: 1454515] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-781, VARIANT ALA-164. Tissue: Uterus.
[10]	"Sp3 is a transcriptional activator of the human alpha2(I) collagen gene." Ihn H., Trojanowska M. Nucleic Acids Res. 25:3712-3717(1997) [PubMed: 9278495] [Abstract] Cited for: FUNCTION.
[11]	"Functional interactions between Sp1 or Sp3 and the helicase-like transcription factor mediate basal expression from the human plasminogen activator inhibitor-1 gene." Ding H., Benotmane A.M., Suske G., Collen D., Belayew A. J. Biol. Chem. 274:19573-19580(1999) [PubMed: 10391891] [Abstract] Cited for: FUNCTION, INTERACTION WITH HLTF.
[12]	"Transcription factor Sp3 is regulated by acetylation." Braun H., Koop R., Ertmer A., Nacht S., Suske G. Nucleic Acids Res. 29:4994-5000(2001) [PubMed: 11812829] [Abstract] Cited for: ACETYLATION AT LYS-551, FUNCTION, MUTAGENESIS OF 551-LYS--GLU-557.
[13]	"The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2." Sun J.M., Chen H.Y., Moniwa M., Litchfield D.W., Seto E., Davie J.R. J. Biol. Chem. 277:35783-35786(2002) [PubMed: 12176973] [Abstract] Cited for: INTERACTION WITH HDAC1 AND HDAC2.
[14]	"SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization." Ross S., Best J.L., Zon L.I., Gill G. Mol. Cell 10:831-842(2002) [PubMed: 12419227] [Abstract] Cited for: SUMOYLATION AT LYS-120 AND LYS-551, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF LYS-120 AND LYS-551.
[15]	"Acetylated SP3 is a transcriptional activator." Ammanamanchi S., Freeman J.W., Brattain M.G. J. Biol. Chem. 278:35775-35780(2003) [PubMed: 12837748] [Abstract] Cited for: INTERACTION WITH HDAC1 AND EP300, ACETYLATION, FUNCTION.
[16]	"Complexity of translationally controlled transcription factor Sp3 isoform expression." Sapetschnig A., Koch F., Rischitor G., Mennenga T., Suske G. J. Biol. Chem. 279:42095-42105(2004) [PubMed: 15247228] [Abstract] Cited for: SUMOYLATION, ALTERNATIVE PRODUCTS, LACK OF GLYCOSYLATION, FUNCTION.
[17]	"Sumoylation of internally initiated Sp3 isoforms regulates transcriptional repression via a Trichostatin A-insensitive mechanism." Spengler M.L., Kennett S.B., Moorefield K.S., Simmons S.O., Brattain M.G., Horowitz J.M. Cell. Signal. 17:153-166(2005) [PubMed: 15494207] [Abstract] Cited for: SUMOYLATION AT LYS-551, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 551-LYS--GLU-553.
[18]	"Sp3 is involved in the regulation of SOCS3 gene expression." Ehlting C., Haussinger D., Bode J.G. Biochem. J. 387:737-745(2005) [PubMed: 15554904] [Abstract] Cited for: ACETYLATION AT LYS-551, FUNCTION.
[19]	"The modification of Sp3 isoforms by SUMOylation has differential effects on the SRC1A promoter." Ellis D.J., Dehm S.M., Bonham K. Gene 379:68-78(2006) [PubMed: 16781829] [Abstract] Cited for: SUMOYLATION AT LYS-551, FUNCTION OF ISOFORMS, MUTAGENESIS OF LYS-551.
[20]	"Nuclear organization and chromatin dynamics--Sp1, Sp3 and histone deacetylases." Davie J.R., He S., Li L., Sekhavat A., Espino P., Drobic B., Dunn K.L., Sun J.M., Chen H.Y., Yu J., Pritchard S., Wang X. Adv. Enzyme Regul. 48:189-208(2008) [PubMed: 18187045] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[21]	"SUMO-modified Sp3 represses transcription by provoking local heterochromatic gene silencing." Stielow B., Sapetschnig A., Wink C., Kraeger I., Suske G. EMBO Rep. 9:899-906(2008) [PubMed: 18617891] [Abstract] Cited for: SUMOYLATION AT LYS-551, FUNCTION OF ISOFORMS.
[22]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-563; SER-566 AND SER-646, MASS SPECTROMETRY.
[23]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, MASS SPECTROMETRY. Tissue: T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY070137 mRNA. Translation: AAL58086.1. AY441957 mRNA. Translation: AAR30505.1. AY441958 mRNA. Translation: AAR30506.1. AK304199 mRNA. Translation: BAG65079.1. BC126414 mRNA. Translation: AAI26415.1. AF494280 Genomic DNA. Translation: AAM12875.1. AJ310752 mRNA. Translation: CAC34575.1. M97191 mRNA. Translation: AAA36630.2. X68560 mRNA. Translation: CAA48562.1.
IPI	IPI00025807. IPI00555936. IPI00852622. IPI00852778. IPI00853491. IPI00853503.
PIR	B44489.
RefSeq	NP_001017371.1. NP_003102.1.
UniGene	Hs.531587
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q02447. 3 interactions.
STRING	Q02447.
PTM databases
PhosphoSite	Q02447.
Proteomic databases
PRIDE	Q02447.
Genome annotation databases
Ensembl	ENST00000310015; ENSP00000310301; ENSG00000172845; Homo sapiens. [Genome view]
GeneID	6670.
KEGG	hsa:6670.
UCSC	uc002uie.1. human. uc002uig.1. human.
Organism-specific databases
CTD	6670.
GeneCards	GC02M174481.
HGNC	HGNC:11208. SP3.
HPA	CAB004580.
MIM	601804. gene.
PharmGKB	PA25068.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q02447.
HOVERGEN	Q02447.
OMA	AGNIVQI
Enzyme and pathway databases
Pathway_Interaction_DB	hnf3bpathway. FOXA2 and FOXA3 transcription factor networks. hif1_tfpathway. HIF-1-alpha transcription factor network. telomerasepathway. Regulation of Telomerase.
Gene expression databases
ArrayExpress	Q02447.
Bgee	Q02447.
CleanEx	HS_SP3.
Genevestigator	Q02447.
GermOnline	ENSG00000172845. Homo sapiens.
Family and domain databases
InterPro	IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
Gene3D	G3DSA:3.30.160.60. Znf_C2H2/integrase_DNA-bd. 2 hits.
Pfam	PF00096. zf-C2H2. 3 hits. [Graphical view]
SMART	SM00355. ZnF_C2H2. 3 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 3 hits. PS50157. ZINC_FINGER_C2H2_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	26005.
PMAP-CutDB	Q02447.
SOURCE	Search...

Entry information

Entry name

SP3_HUMAN

Accession

Primary (citable) accession number: Q02447
Secondary accession number(s): A0AVL9 , B4E2B7, Q69B26, Q69B27, Q8TD56, Q8WWU4, Q9BQR1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	May 16, 2003
Last modified:	November 24, 2009
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.