Q12800 (TFCP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-globin transcription factor CP2

Alternative name(s):
SAA3 enhancer factor
Transcription factor LSF

Gene names

Name:	TFCP2
Synonyms:	LSF, SEF

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	502 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.7. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Traceable author statement Ref.3. Source: ProtInc sequence-specific DNA binding transcription factor activity Traceable author statement Ref.7. Source: ProtInc
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 502	502	Alpha-globin transcription factor CP2		PRO_0000228001
Regions
	Region	133 – 395	263	DNA-binding
	Compositional bias	314 – 319	6	Poly-Pro
	Compositional bias	396 – 413	18	Gln-rich
Natural variations
	Alternative sequence	189 – 239	51	Missing in isoform 2 and isoform 3.		VSP_017647
	Alternative sequence	491	1	Missing in isoform 2 and isoform 4.		VSP_017648
Experimental info
	Mutagenesis	211	1	V → E: Does not affect DNA-binding activity. Ref.3
	Mutagenesis	213	1	I → R: Does not affect DNA-binding activity. Ref.3
	Mutagenesis	234	1	Q → L: Significant reduction of DNA-binding activity. Ref.3
	Mutagenesis	236	1	K → E: Significant reduction of DNA-binding activity. Ref.3
	Sequence conflict	92	1	G → A in M84810. Ref.1
	Sequence conflict	92	1	G → A AA sequence Ref.1
	Sequence conflict	249	1	T → M in M84810. Ref.1
	Sequence conflict	249	1	T → M AA sequence Ref.1
	Sequence conflict	491	1	A → Q in AAA21324. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (LBP-1c) [UniParc]. Last modified March 21, 2006. Version 2. Checksum: B93825C2687F89FF	FASTA	502	57,256
	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
	Isoform 2 [UniParc]. Checksum: 5004E9DF3925E852	FASTA	450	51,308
	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 KRTSVFIQPK GADRKQKTDR EKMEKRTPHE KEKYQPSYET TILTECSPWP EITYVNNSPS 250 260 270 280 290 300 PGFNSSHSSF SLGEGNGSPN HQPEPPPPVT DNLLPTTTPQ EAQQWLHRNR FSTFTRLFTN 310 320 330 340 350 360 FSGADLLKLT RDDVIQICGP ADGIRLFNAL KGRMVRPRLT IYVCQESLQL REQQQQQQQQ 370 380 390 400 410 420 QQKHEDGDSN GTFFVYHAIY LEELTAVELT EKIAQLFSIS PCQISQIYKQ GPTGIHVLIS 430 440 450 DEMIQNFQEE ACFILDTMKE TNDSYHIILK
	Isoform 3 (LBP-1d) [UniParc]. Checksum: 04DAF489CA939B17	FASTA	451	51,379
	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 KRTSVFIQPK GADRKQKTDR EKMEKRTPHE KEKYQPSYET TILTECSPWP EITYVNNSPS 250 260 270 280 290 300 PGFNSSHSSF SLGEGNGSPN HQPEPPPPVT DNLLPTTTPQ EAQQWLHRNR FSTFTRLFTN 310 320 330 340 350 360 FSGADLLKLT RDDVIQICGP ADGIRLFNAL KGRMVRPRLT IYVCQESLQL REQQQQQQQQ 370 380 390 400 410 420 QQKHEDGDSN GTFFVYHAIY LEELTAVELT EKIAQLFSIS PCQISQIYKQ GPTGIHVLIS 430 440 450 DEMIQNFQEE ACFILDTMKA ETNDSYHIIL K
	Isoform 4 [UniParc]. Checksum: 22D5A27DD537009D	FASTA	501	57,185
	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 ETNDSYHIIL K

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00037599. IPI00140998. IPI00791184. IPI00953927.
PIR	A42030. A53771. C56205.
RefSeq	NP_001166923.1. NM_001173452.1. NP_001166924.1. NM_001173453.1. NP_005644.2. NM_005653.4.
UniGene	Hs.48849.
3D structure databases
ProteinModelPortal	Q12800.
SMR	Q12800. Positions 322-383.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12800. 34 interactions.
MINT	MINT-1388673.
STRING	9606.ENSP00000257915.
PTM databases
PhosphoSite	Q12800.
Polymorphism databases
DMDM	90101767.
Proteomic databases
PaxDb	Q12800.
PRIDE	Q12800.
Protocols and materials databases
DNASU	7024.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000257915; ENSP00000257915; ENSG00000135457. ENST00000307660; ENSP00000304411; ENSG00000135457. ENST00000548115; ENSP00000447991; ENSG00000135457.
GeneID	7024.
KEGG	hsa:7024.
UCSC	uc001rxv.2. human. uc001rxw.3. human. uc009zlx.2. human.
Organism-specific databases
CTD	7024.
GeneCards	GC12M051488.
HGNC	HGNC:11748. TFCP2.
MIM	189889. gene.
neXtProt	NX_Q12800.
PharmGKB	PA36463.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG275458.
HOGENOM	HOG000230625.
HOVERGEN	HBG053805.
InParanoid	Q12800.
KO	K09275.
OMA	FKQEESN.
OrthoDB	EOG4K3KW2.
PhylomeDB	Q12800.
Enzyme and pathway databases
Pathway_Interaction_DB	hdac_classi_pathway. Signaling events mediated by HDAC Class I.
Gene expression databases
ArrayExpress	Q12800.
Bgee	Q12800.
CleanEx	HS_TFCP2.
Genevestigator	Q12800.
GermOnline	ENSG00000135457. Homo sapiens.
Family and domain databases
InterPro	IPR007604. CP2. IPR013761. SAM/pointed. [Graphical view]
Pfam	PF04516. CP2. 1 hit. [Graphical view]
SUPFAM	SSF47769. SAM_homology. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	7024.
NextBio	27443.
SOURCE	Search...

Entry information

Entry name

TFCP2_HUMAN

Accession

Primary (citable) accession number: Q12800
Secondary accession number(s): A8K5E9 , Q12801, Q9UD75, Q9UD77

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	March 21, 2006
Last modified:	April 3, 2013
This is version 95 of the entry and version 2 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.