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Protein

Transcription factor 20

Gene

TCF20

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi1537 – 155115A.T hookAdd
BLAST
Zinc fingeri1884 – 193552PHD-type; atypicalAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: GO_Central
  • transcription regulatory region DNA binding Source: GO_Central
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor 20
Short name:
TCF-20
Alternative name(s):
Nuclear factor SPBP
Protein AR1
Stromelysin-1 PDGF-responsive element-binding protein
Short name:
SPRE-binding protein
Gene namesi
Name:TCF20
Synonyms:KIAA0292, SPBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:11631. TCF20.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36386.

Polymorphism and mutation databases

BioMutaiTCF20.
DMDMi92090378.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19601960Transcription factor 20PRO_0000072448Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei419 – 4191PhosphoserineCombined sources
Modified residuei430 – 4301PhosphoserineCombined sources
Modified residuei574 – 5741PhosphoserineCombined sources
Modified residuei583 – 5831PhosphoserineCombined sources
Modified residuei602 – 6021N6-acetyllysineBy similarity
Cross-linki710 – 710Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki823 – 823Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki844 – 844Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei871 – 8711PhosphoserineCombined sources
Cross-linki929 – 929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki957 – 957Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei966 – 9661PhosphoserineCombined sources
Modified residuei1053 – 10531PhosphoserineCombined sources
Cross-linki1137 – 1137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1335 – 13351PhosphoserineCombined sources
Modified residuei1361 – 13611PhosphoserineCombined sources
Cross-linki1446 – 1446Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1522 – 15221PhosphoserineCombined sources
Modified residuei1669 – 16691PhosphoserineCombined sources
Modified residuei1671 – 16711PhosphothreonineCombined sources
Modified residuei1762 – 17621PhosphothreonineBy similarity
Modified residuei1764 – 17641PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UGU0.
PaxDbiQ9UGU0.
PRIDEiQ9UGU0.

PTM databases

iPTMnetiQ9UGU0.
PhosphoSiteiQ9UGU0.

Miscellaneous databases

PMAP-CutDBQ9UGU0.

Expressioni

Tissue specificityi

Expressed in most tissues, except in ovary and prostate. Isoform 1 is exclusively expressed in brain, heart and testis, and this form predominates in liver and kidney. Isoform 2 predominates in lung.

Gene expression databases

BgeeiQ9UGU0.
CleanExiHS_TCF20.
ExpressionAtlasiQ9UGU0. baseline and differential.
GenevisibleiQ9UGU0. HS.

Organism-specific databases

HPAiCAB017849.
HPA036786.

Interactioni

Subunit structurei

Homodimer (Probable). Interacts with RNF4 and JUN (By similarity).By similarityCurated

Protein-protein interaction databases

BioGridi112802. 37 interactions.
IntActiQ9UGU0. 28 interactions.
MINTiMINT-4541027.
STRINGi9606.ENSP00000352463.

Structurei

3D structure databases

ProteinModelPortaliQ9UGU0.
SMRiQ9UGU0. Positions 1848-1932.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1170 – 119122Leucine-zipperAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1254 – 126815Nuclear localization signalBy similarityAdd
BLAST
Motifi1576 – 160025Nuclear localization signalBy similarityAdd
BLAST
Motifi1785 – 17928Nuclear localization signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi62 – 709Poly-Ala
Compositional biasi174 – 1829Poly-Gln
Compositional biasi203 – 26260Ser-richAdd
BLAST
Compositional biasi310 – 32213Poly-GlnAdd
BLAST
Compositional biasi1556 – 15649Poly-Pro

Domaini

The atypical PHD domain functions as a negative modulator of cofactor binding.By similarity

Sequence similaritiesi

Contains 1 A.T hook DNA-binding domain.Curated
Contains 1 PHD-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1884 – 193552PHD-type; atypicalAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IPTF. Eukaryota.
ENOG410ZTQQ. LUCA.
GeneTreeiENSGT00530000063684.
HOGENOMiHOG000026801.
HOVERGENiHBG079232.
InParanoidiQ9UGU0.
OMAiEVLQGYH.
PhylomeDBiQ9UGU0.
TreeFamiTF331317.

Family and domain databases

InterProiIPR001965. Znf_PHD.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UGU0-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MQSFREQSSY HGNQQSYPQE VHGSSRLEEF SPRQAQMFQN FGGTGGSSGS
60 70 80 90 100
SGSGSGGGRR GAAAAAAAMA SETSGHQGYQ GFRKEAGDFY YMAGNKDPVT
110 120 130 140 150
TGTPQPPQRR PSGPVQSYGP PQGSSFGNQY GSEGHVGQFQ AQHSGLGGVS
160 170 180 190 200
HYQQDYTGPF SPGSAQYQQQ ASSQQQQQQV QQLRQQLYQS HQPLPQATGQ
210 220 230 240 250
PASSSSHLQP MQRPSTLPSS AAGYQLRVGQ FGQHYQSSAS SSSSSSFPSP
260 270 280 290 300
QRFSQSGQSY DGSYNVNAGS QYEGHNVGSN AQAYGTQSNY SYQPQSMKNF
310 320 330 340 350
EQAKIPQGTQ QGQQQQQPQQ QQHPSQHVMQ YTNAATKLPL QSQVGQYNQP
360 370 380 390 400
EVPVRSPMQF HQNFSPISNP SPAASVVQSP SCSSTPSPLM QTGENLQCGQ
410 420 430 440 450
GSVPMGSRNR ILQLMPQLSP TPSMMPSPNS HAAGFKGFGL EGVPEKRLTD
460 470 480 490 500
PGLSSLSALS TQVANLPNTV QHMLLSDALT PQKKTSKRPS SSKKADSCTN
510 520 530 540 550
SEGSSQPEEQ LKSPMAESLD GGCSSSSEDQ GERVRQLSGQ STSSDTTYKG
560 570 580 590 600
GASEKAGSSP AQGAQNEPPR LNASPAAREE ATSPGAKDMP LSSDGNPKVN
610 620 630 640 650
EKTVGVIVSR EAMTGRVEKP GGQDKGSQED DPAATQRPPS NGGAKETSHA
660 670 680 690 700
SLPQPEPPGG GGSKGNKNGD NNSNHNGEGN GQSGHSAAGP GFTSRTEPSK
710 720 730 740 750
SPGSLRYSYK DSFGSAVPRN VSGFPQYPTG QEKGDFTGHG ERKGRNEKFP
760 770 780 790 800
SLLQEVLQGY HHHPDRRYSR STQEHQGMAG SLEGTTRPNV LVSQTNELAS
810 820 830 840 850
RGLLNKSIGS LLENPHWGPW ERKSSSTAPE MKQINLTDYP IPRKFEIEPQ
860 870 880 890 900
SSAHEPGGSL SERRSVICDI SPLRQIVRDP GAHSLGHMSA DTRIGRNDRL
910 920 930 940 950
NPTLSQSVIL PGGLVSMETK LKSQSGQIKE EDFEQSKSQA SFNNKKSGDH
960 970 980 990 1000
CHPPSIKHES YRGNASPGAA THDSLSDYGP QDSRPTPMRR VPGRVGGREG
1010 1020 1030 1040 1050
MRGRSPSQYH DFAEKLKMSP GRSRGPGGDP HHMNPHMTFS ERANRSSLHT
1060 1070 1080 1090 1100
PFSPNSETLA SAYHANTRAH AYGDPNAGLN SQLHYKRQMY QQQPEEYKDW
1110 1120 1130 1140 1150
SSGSAQGVIA AAQHRQEGPR KSPRQQQFLD RVRSPLKNDK DGMMYGPPVG
1160 1170 1180 1190 1200
TYHDPSAQEA GRCLMSSDGL PNKGMELKHG SQKLQESCWD LSRQTSPAKS
1210 1220 1230 1240 1250
SGPPGMSSQK RYGPPHETDG HGLAEATQSS KPGSVMLRLP GQEDHSSQNP
1260 1270 1280 1290 1300
LIMRRRVRSF ISPIPSKRQS QDVKNSSTED KGRLLHSSKE GADKAFNSYA
1310 1320 1330 1340 1350
HLSHSQDIKS IPKRDSSKDL PSPDSRNCPA VTLTSPAKTK ILPPRKGRGL
1360 1370 1380 1390 1400
KLEAIVQKIT SPNIRRSASS NSAEAGGDTV TLDDILSLKS GPPEGGSVAV
1410 1420 1430 1440 1450
QDADIEKRKG EVASDLVSPA NQELHVEKPL PRSSEEWRGS VDDKVKTETH
1460 1470 1480 1490 1500
AETVTAGKEP PGAMTSTTSQ KPGSNQGRPD GSLGGTAPLI FPDSKNVPPV
1510 1520 1530 1540 1550
GILAPEANPK AEEKENDTVT ISPKQEGFPP KGYFPSGKKK GRPIGSVNKQ
1560 1570 1580 1590 1600
KKQQQPPPPP PQPPQIPEGS ADGEPKPKKQ RQRRERRKPG AQPRKRKTKQ
1610 1620 1630 1640 1650
AVPIVEPQEP EIKLKYATQP LDKTDAKNKS FYPYIHVVNK CELGAVCTII
1660 1670 1680 1690 1700
NAEEEEQTKL VRGRKGQRSL TPPPSSTESK ALPASSFMLQ GPVVTESSVM
1710 1720 1730 1740 1750
GHLVCCLCGK WASYRNMGDL FGPFYPQDYA ATLPKNPPPK RATEMQSKVK
1760 1770 1780 1790 1800
VRHKSASNGS KTDTEEEEEQ QQQQKEQRSL AAHPRFKRRH RSEDCGGGPR
1810 1820 1830 1840 1850
SLSRGLPCKK AATEGSSEKT VLDSKPSVPT TSEGGPELEL QIPELPLDSN
1860 1870 1880 1890 1900
EFWVHEGCIL WANGIYLVCG RLYGLQEALE IAREMKCSHC QEAGATLGCY
1910 1920 1930 1940 1950
NKGCSFRYHY PCAIDADCLL HEENFSVRCP KHKPPLPCPL PPLQNKTAKG
1960
SLSTEQSERG
Length:1,960
Mass (Da):211,771
Last modified:March 7, 2006 - v3
Checksum:iD3E34B1FAA6ED06F
GO
Isoform 2 (identifier: Q9UGU0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1934-1938: PPLPC → VRLWR
     1939-1960: Missing.

Show »
Length:1,938
Mass (Da):209,654
Checksum:iDB67ACCB0AE5776C
GO

Sequence cautioni

The sequence AAC36392.1 differs from that shown. Reason: Frameshift at position 1932. Curated
The sequence CAB42440.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221Q → R (PubMed:10995766).Curated
Sequence conflicti200 – 2001Q → K (PubMed:10995766).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti405 – 4051M → V.
Corresponds to variant rs34030679 [ dbSNP | Ensembl ].
VAR_051419
Natural varianti485 – 4851T → N.
Corresponds to variant rs6002656 [ dbSNP | Ensembl ].
VAR_025427
Natural varianti722 – 7221S → G.
Corresponds to variant rs5758651 [ dbSNP | Ensembl ].
VAR_025428
Natural varianti1165 – 11651M → I.
Corresponds to variant rs17002890 [ dbSNP | Ensembl ].
VAR_025429
Natural varianti1325 – 13251S → N.
Corresponds to variant rs17002888 [ dbSNP | Ensembl ].
VAR_025430
Natural varianti1910 – 19101Y → C.
Corresponds to variant rs17002865 [ dbSNP | Ensembl ].
VAR_051420

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1934 – 19385PPLPC → VRLWR in isoform 2. 1 PublicationVSP_003984
Alternative sequencei1939 – 196022Missing in isoform 2. 1 PublicationVSP_003985Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007595 Genomic DNA. Translation: AAG28930.1.
AL031346 Genomic DNA. Translation: CAB42440.1. Different initiation.
BX247885 Genomic DNA. Translation: CAI95721.1.
BX247885 Genomic DNA. Translation: CAP58858.1.
CH471095 Genomic DNA. Translation: EAW60495.1.
AB006630 mRNA. Translation: BAA22961.1.
U19345 mRNA. Translation: AAC36392.1. Frameshift.
CCDSiCCDS14032.1. [Q9UGU0-2]
CCDS14033.1. [Q9UGU0-1]
RefSeqiNP_005641.1. NM_005650.3. [Q9UGU0-1]
NP_852469.1. NM_181492.2. [Q9UGU0-2]
XP_005261779.1. XM_005261722.2. [Q9UGU0-1]
XP_006724376.1. XM_006724313.2. [Q9UGU0-1]
XP_011528656.1. XM_011530354.1. [Q9UGU0-2]
UniGeneiHs.475018.

Genome annotation databases

EnsembliENST00000335626; ENSP00000335561; ENSG00000100207. [Q9UGU0-2]
ENST00000359486; ENSP00000352463; ENSG00000100207. [Q9UGU0-1]
ENST00000574943; ENSP00000460328; ENSG00000262024. [Q9UGU0-1]
ENST00000576946; ENSP00000460587; ENSG00000262024. [Q9UGU0-2]
ENST00000619505; ENSP00000478503; ENSG00000276461. [Q9UGU0-2]
ENST00000621408; ENSP00000483199; ENSG00000276461. [Q9UGU0-1]
ENST00000626486; ENSP00000487465; ENSG00000280467. [Q9UGU0-2]
ENST00000626726; ENSP00000487302; ENSG00000281897. [Q9UGU0-1]
ENST00000628774; ENSP00000487296; ENSG00000280467. [Q9UGU0-1]
ENST00000629538; ENSP00000486940; ENSG00000281897. [Q9UGU0-2]
ENST00000634489; ENSP00000489099; ENSG00000282892. [Q9UGU0-2]
ENST00000634616; ENSP00000489614; ENSG00000283026. [Q9UGU0-1]
ENST00000635146; ENSP00000489215; ENSG00000282892. [Q9UGU0-1]
ENST00000635421; ENSP00000489006; ENSG00000283026. [Q9UGU0-2]
GeneIDi6942.
KEGGihsa:6942.
UCSCiuc003bck.3. human. [Q9UGU0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007595 Genomic DNA. Translation: AAG28930.1.
AL031346 Genomic DNA. Translation: CAB42440.1. Different initiation.
BX247885 Genomic DNA. Translation: CAI95721.1.
BX247885 Genomic DNA. Translation: CAP58858.1.
CH471095 Genomic DNA. Translation: EAW60495.1.
AB006630 mRNA. Translation: BAA22961.1.
U19345 mRNA. Translation: AAC36392.1. Frameshift.
CCDSiCCDS14032.1. [Q9UGU0-2]
CCDS14033.1. [Q9UGU0-1]
RefSeqiNP_005641.1. NM_005650.3. [Q9UGU0-1]
NP_852469.1. NM_181492.2. [Q9UGU0-2]
XP_005261779.1. XM_005261722.2. [Q9UGU0-1]
XP_006724376.1. XM_006724313.2. [Q9UGU0-1]
XP_011528656.1. XM_011530354.1. [Q9UGU0-2]
UniGeneiHs.475018.

3D structure databases

ProteinModelPortaliQ9UGU0.
SMRiQ9UGU0. Positions 1848-1932.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112802. 37 interactions.
IntActiQ9UGU0. 28 interactions.
MINTiMINT-4541027.
STRINGi9606.ENSP00000352463.

PTM databases

iPTMnetiQ9UGU0.
PhosphoSiteiQ9UGU0.

Polymorphism and mutation databases

BioMutaiTCF20.
DMDMi92090378.

Proteomic databases

EPDiQ9UGU0.
PaxDbiQ9UGU0.
PRIDEiQ9UGU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335626; ENSP00000335561; ENSG00000100207. [Q9UGU0-2]
ENST00000359486; ENSP00000352463; ENSG00000100207. [Q9UGU0-1]
ENST00000574943; ENSP00000460328; ENSG00000262024. [Q9UGU0-1]
ENST00000576946; ENSP00000460587; ENSG00000262024. [Q9UGU0-2]
ENST00000619505; ENSP00000478503; ENSG00000276461. [Q9UGU0-2]
ENST00000621408; ENSP00000483199; ENSG00000276461. [Q9UGU0-1]
ENST00000626486; ENSP00000487465; ENSG00000280467. [Q9UGU0-2]
ENST00000626726; ENSP00000487302; ENSG00000281897. [Q9UGU0-1]
ENST00000628774; ENSP00000487296; ENSG00000280467. [Q9UGU0-1]
ENST00000629538; ENSP00000486940; ENSG00000281897. [Q9UGU0-2]
ENST00000634489; ENSP00000489099; ENSG00000282892. [Q9UGU0-2]
ENST00000634616; ENSP00000489614; ENSG00000283026. [Q9UGU0-1]
ENST00000635146; ENSP00000489215; ENSG00000282892. [Q9UGU0-1]
ENST00000635421; ENSP00000489006; ENSG00000283026. [Q9UGU0-2]
GeneIDi6942.
KEGGihsa:6942.
UCSCiuc003bck.3. human. [Q9UGU0-1]

Organism-specific databases

CTDi6942.
GeneCardsiTCF20.
H-InvDBHIX0016540.
HGNCiHGNC:11631. TCF20.
HPAiCAB017849.
HPA036786.
MIMi603107. gene.
neXtProtiNX_Q9UGU0.
PharmGKBiPA36386.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPTF. Eukaryota.
ENOG410ZTQQ. LUCA.
GeneTreeiENSGT00530000063684.
HOGENOMiHOG000026801.
HOVERGENiHBG079232.
InParanoidiQ9UGU0.
OMAiEVLQGYH.
PhylomeDBiQ9UGU0.
TreeFamiTF331317.

Miscellaneous databases

ChiTaRSiTCF20. human.
GeneWikiiTCF20.
GenomeRNAii6942.
NextBioi27171.
PMAP-CutDBQ9UGU0.
PROiQ9UGU0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UGU0.
CleanExiHS_TCF20.
ExpressionAtlasiQ9UGU0. baseline and differential.
GenevisibleiQ9UGU0. HS.

Family and domain databases

InterProiIPR001965. Znf_PHD.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nuclear factor SPBP contains different functional domains and stimulates the activity of various transcriptional activators."
    Rekdal C., Sjoettem E., Johansen T.
    J. Biol. Chem. 275:40288-40300(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), CHARACTERIZATION, ALTERNATIVE SPLICING.
  2. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins."
    Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.
    DNA Res. 4:53-59(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-1960 (ISOFORM 1).
    Tissue: Brain.
  5. "Assignment of AR1, transcription factor 20 (TCF20), to human chromosome 22q13.3 with somatic cell hybrids and in situ hybridization."
    Rajadhyaksha A., Riviere M., Van Vooren P., Szpirer J., Szpirer C., Babin J., Bina M.
    Cytogenet. Cell Genet. 81:176-177(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1083-1938 (ISOFORM 2).
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-574; SER-583; SER-871; SER-1335; SER-1361; SER-1522; SER-1669 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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].
  8. "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-419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-871; SER-966; SER-1053; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-823; LYS-844; LYS-929 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-710; LYS-844; LYS-929 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-823; LYS-844; LYS-929; LYS-957; LYS-1137 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTCF20_HUMAN
AccessioniPrimary (citable) accession number: Q9UGU0
Secondary accession number(s): A9JX12
, O14528, Q13078, Q4V353, Q9H4M0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: March 7, 2006
Last modified: April 13, 2016
This is version 131 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. 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.