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Q12800 (TFCP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-globin transcription factor CP2
Alternative name(s):
SAA3 enhancer factor
Transcription factor LSF
Gene names
Name:TFCP2
Synonyms:LSF, SEF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds a variety of cellular and viral promoters including fibrinogen, alpha-globin, SV40 and HIV-1 promoters. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with UBP1 By similarity. Functions as part of the SSP (stage selector protein) complex. Facilitates the interaction of the gamma-globin genes with enhancer elements contained in the locus control region in fetal erythroid cells. Interacts by binding to the stage selector element (SSE) in the proximal gamma-globin promoter. Ref.1 Ref.3 Ref.7 Ref.10

Subunit structure

Binds to DNA as a dimer, isoform 3 does not bind to DNA or affect the binding of isoform 1 to DNA. Interacts with UBP1 and PIAS1, and is probably part of a complex containing TFCP2, UBP1 and PIAS1 By similarity. Component of the SSP (stage selector protein) complex, which appears to be a heteromer of TFCP2 and 2 copies of NFE4. Ref.8 Ref.11

Subcellular location

Nucleus Ref.1 Ref.2 Ref.8.

Tissue specificity

Ubiquitous. Expressed in brain, ovary, kidney, thymus, spleen, liver, adrenal, heart and lung (at protein level). Ref.7 Ref.8 Ref.10

Developmental stage

Expressed in fetal erythroid tissue. Ref.7 Ref.8

Miscellaneous

In Ref.2 authors noted that a 10-fold molar excess of isoform 3 over isoform 1 inhibited DNA-binding.

Sequence similarities

Belongs to the grh/CP2 family. CP2 subfamily.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12800-1)

Also known as: LBP-1c;

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: Q12800-2)

The sequence of this isoform differs from the canonical sequence as follows:
     189-239: Missing.
     491-491: Missing.
Isoform 3 (identifier: Q12800-3)

Also known as: LBP-1d;

The sequence of this isoform differs from the canonical sequence as follows:
     189-239: Missing.
Isoform 4 (identifier: Q12800-4)

The sequence of this isoform differs from the canonical sequence as follows:
     491-491: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 502502Alpha-globin transcription factor CP2
PRO_0000228001

Regions

Region133 – 395263DNA-binding
Compositional bias314 – 3196Poly-Pro
Compositional bias396 – 41318Gln-rich

Natural variations

Alternative sequence189 – 23951Missing in isoform 2 and isoform 3.
VSP_017647
Alternative sequence4911Missing in isoform 2 and isoform 4.
VSP_017648

Experimental info

Mutagenesis2111V → E: Does not affect DNA-binding activity. Ref.3
Mutagenesis2131I → R: Does not affect DNA-binding activity. Ref.3
Mutagenesis2341Q → L: Significant reduction of DNA-binding activity. Ref.3
Mutagenesis2361K → E: Significant reduction of DNA-binding activity. Ref.3
Sequence conflict921G → A in M84810. Ref.1
Sequence conflict921G → A AA sequence Ref.1
Sequence conflict2491T → M in M84810. Ref.1
Sequence conflict2491T → M AA sequence Ref.1
Sequence conflict4911A → Q in AAA21324. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LBP-1c) [UniParc].

Last modified March 21, 2006. Version 2.
Checksum: B93825C2687F89FF

FASTA50257,256
        10         20         30         40         50         60 
MAWALKLPLA DEVIESGLVQ DFDASLSGIG QELGAGAYSM SDVLALPIFK QEESSLPPDN 

        70         80         90        100        110        120 
ENKILPFQYV LCAATSPAVK LHDETLTYLN QGQSYEIRML DNRKLGELPE INGKLVKSIF 

       130        140        150        160        170        180 
RVVFHDRRLQ YTEHQQLEGW RWNRPGDRIL DIDIPMSVGI IDPRANPTQL NTVEFLWDPA 

       190        200        210        220        230        240 
KRTSVFIQVH CISTEFTMRK HGGEKGVPFR VQIDTFKENE NGEYTEHLHS ASCQIKVFKP 

       250        260        270        280        290        300 
KGADRKQKTD REKMEKRTPH EKEKYQPSYE TTILTECSPW PEITYVNNSP SPGFNSSHSS 

       310        320        330        340        350        360 
FSLGEGNGSP NHQPEPPPPV TDNLLPTTTP QEAQQWLHRN RFSTFTRLFT NFSGADLLKL 

       370        380        390        400        410        420 
TRDDVIQICG PADGIRLFNA LKGRMVRPRL TIYVCQESLQ LREQQQQQQQ QQQKHEDGDS 

       430        440        450        460        470        480 
NGTFFVYHAI YLEELTAVEL TEKIAQLFSI SPCQISQIYK QGPTGIHVLI SDEMIQNFQE 

       490        500 
EACFILDTMK AETNDSYHII LK 

« Hide

Isoform 2 [UniParc].

Checksum: 5004E9DF3925E852
Show »

FASTA45051,308
Isoform 3 (LBP-1d) [UniParc].

Checksum: 04DAF489CA939B17
Show »

FASTA45151,379
Isoform 4 [UniParc].

Checksum: 22D5A27DD537009D
Show »

FASTA50157,185

References

« Hide 'large scale' references
[1]"Molecular cloning of the alpha-globin transcription factor CP2."
Lim L.C., Swendeman S.L., Sheffery M.
Mol. Cell. Biol. 12:828-835(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF 129-140; 165-176; 348-358 AND 390-397, FUNCTION, SUBCELLULAR LOCATION.
[2]"Characterization of a family of related cellular transcription factors which can modulate human immunodeficiency virus type 1 transcription in vitro."
Yoon J.-B., Li G., Roeder R.G.
Mol. Cell. Biol. 14:1776-1785(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 61-502 (ISOFORM 3), DNA-BINDING, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
[3]"One exon of the human LSF gene includes conserved regions involved in novel DNA-binding and dimerization motifs."
Shirra M.K., Zhu Q., Huang H.-C., Pallas D., Hansen U.
Mol. Cell. Biol. 14:5076-5087(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 7-21; 81-98; 149-164; 165-179; 348-359 AND 363-376, FUNCTION, ALTERNATIVE SPLICING, MUTAGENESIS OF VAL-211; ILE-213; GLN-234 AND LYS-236.
[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. expand/collapse author list , 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] (ISOFORM 4).
Tissue: Teratocarcinoma.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Muscle.
[7]"Characterization of the genomic structure, chromosomal location, promoter, and development expression of the alpha-globin transcription factor CP2."
Swendeman S.L., Spielholz C., Jenkins N.A., Gilbert D.J., Copeland N.G., Sheffery M.
J. Biol. Chem. 269:11663-11671(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]"Hemoglobin switching in man and chicken is mediated by a heteromeric complex between the ubiquitous transcription factor CP2 and a developmentally specific protein."
Jane S.M., Nienhuis A.W., Cunningham J.M.
EMBO J. 14:97-105(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SSP COMPLEX, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[9]Erratum
Jane S.M., Nienhuis A.W., Cunningham J.M.
EMBO J. 15:854-855(1995)
[10]"Purification and characterization of the serum amyloid A3 enhancer factor."
Bing Z., Reddy S.A., Ren Y., Qin J., Liao W.S.-L.
J. Biol. Chem. 274:24649-24656(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[11]"Induction of human fetal globin gene expression by a novel erythroid factor, NF-E4."
Zhou W., Clouston D.R., Wang X., Cerruti L., Cunningham J.M., Jane S.M.
Mol. Cell. Biol. 20:7662-7672(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFE4.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84810 mRNA. No translation available.
U03494 mRNA. Translation: AAA21324.1.
U03495 mRNA. Translation: AAA21325.1.
AK291264 mRNA. Translation: BAF83953.1.
CH471111 Genomic DNA. Translation: EAW58178.1.
BC003634 mRNA. Translation: AAH03634.1.
PIRA42030.
A53771.
C56205.
RefSeqNP_001166923.1. NM_001173452.1.
NP_001166924.1. NM_001173453.1.
NP_005644.2. NM_005653.4.
UniGeneHs.48849.

3D structure databases

ProteinModelPortalQ12800.
SMRQ12800. Positions 322-382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112882. 19 interactions.
IntActQ12800. 38 interactions.
MINTMINT-1388673.
STRING9606.ENSP00000257915.

PTM databases

PhosphoSiteQ12800.

Polymorphism databases

DMDM90101767.

Proteomic databases

PaxDbQ12800.
PRIDEQ12800.

Protocols and materials databases

DNASU7024.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257915; ENSP00000257915; ENSG00000135457. [Q12800-1]
ENST00000307660; ENSP00000304411; ENSG00000135457. [Q12800-3]
ENST00000548115; ENSP00000447991; ENSG00000135457. [Q12800-2]
GeneID7024.
KEGGhsa:7024.
UCSCuc001rxv.2. human. [Q12800-4]
uc001rxw.3. human. [Q12800-1]
uc009zlx.2. human. [Q12800-2]

Organism-specific databases

CTD7024.
GeneCardsGC12M051488.
HGNCHGNC:11748. TFCP2.
MIM189889. gene.
neXtProtNX_Q12800.
PharmGKBPA36463.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG275458.
HOGENOMHOG000230625.
HOVERGENHBG053805.
InParanoidQ12800.
KOK09275.
OMADEVCFVL.
OrthoDBEOG7FBRHB.
PhylomeDBQ12800.
TreeFamTF314132.

Gene expression databases

ArrayExpressQ12800.
BgeeQ12800.
CleanExHS_TFCP2.
GenevestigatorQ12800.

Family and domain databases

InterProIPR007604. CP2.
IPR013761. SAM/pointed.
[Graphical view]
PfamPF04516. CP2. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
ProtoNetSearch...

Other

GeneWikiTFCP2.
GenomeRNAi7024.
NextBio27443.
PROQ12800.
SOURCESearch...

Entry information

Entry nameTFCP2_HUMAN
AccessionPrimary (citable) accession number: Q12800
Secondary accession number(s): A8K5E9 expand/collapse secondary AC list , Q12801, Q9UD75, Q9UD77
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: March 19, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM