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Protein

Alpha-globin transcription factor CP2

Gene

TFCP2

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

Functioni

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.By similarity4 Publications

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • protein C-terminus binding Source: UniProtKB
  • sequence-specific DNA binding Source: GO_Central
  • sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-globin transcription factor CP2
Alternative name(s):
SAA3 enhancer factor
Transcription factor LSF
Gene namesi
Name:TFCP2
Synonyms:LSF, SEF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:11748. TFCP2.

Subcellular locationi

  • Nucleus 3 Publications

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi211 – 2111V → E: Does not affect DNA-binding activity. 1 Publication
Mutagenesisi213 – 2131I → R: Does not affect DNA-binding activity. 1 Publication
Mutagenesisi234 – 2341Q → L: Significant reduction of DNA-binding activity. 1 Publication
Mutagenesisi236 – 2361K → E: Significant reduction of DNA-binding activity. 1 Publication

Organism-specific databases

PharmGKBiPA36463.

Polymorphism and mutation databases

BioMutaiTFCP2.
DMDMi90101767.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Alpha-globin transcription factor CP2PRO_0000228001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei353 – 3531Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12800.
PaxDbiQ12800.
PRIDEiQ12800.

PTM databases

PhosphoSiteiQ12800.

Expressioni

Tissue specificityi

Ubiquitous. Expressed in brain, ovary, kidney, thymus, spleen, liver, adrenal, heart and lung (at protein level).3 Publications

Developmental stagei

Expressed in fetal erythroid tissue.2 Publications

Gene expression databases

BgeeiQ12800.
CleanExiHS_TFCP2.
ExpressionAtlasiQ12800. baseline and differential.
GenevisibleiQ12800. HS.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADPRHP549223EBI-717422,EBI-6657604
ASAP3Q8TDY43EBI-717422,EBI-2609717
BAG6P463793EBI-717422,EBI-347552
C19orf73Q9NVV23EBI-717422,EBI-2859285
CA1P009153EBI-717422,EBI-3912102
CBX8Q9HC523EBI-717422,EBI-712912
CCDC94Q9BW853EBI-717422,EBI-10300345
CDC73Q6P1J95EBI-717422,EBI-930143
CGI-87Q53QD43EBI-717422,EBI-10242701
DNAJC27Q9NZQ03EBI-717422,EBI-10317544
DNAJC5BQ9UF473EBI-717422,EBI-10320535
DPH1Q9BZG83EBI-717422,EBI-10303200
E2F8A0AVK63EBI-717422,EBI-7779316
EAF1Q96JC93EBI-717422,EBI-769261
EIF5BQ8N5A03EBI-717422,EBI-6137508
EPHA10Q5JZY3-33EBI-717422,EBI-10244652
FAM64AQ9BSJ63EBI-717422,EBI-2568609
FANCLQ9NW383EBI-717422,EBI-2339898
FARS2O953633EBI-717422,EBI-2513774
FBXL18Q96D163EBI-717422,EBI-744419
GPANK1O958723EBI-717422,EBI-751540
IRAK1BP1Q5VVH53EBI-717422,EBI-9658404
KIAA1598A0MZ66-73EBI-717422,EBI-10171490
MOB3CQ70IA83EBI-717422,EBI-9679267
MORF4L1Q9UBU83EBI-717422,EBI-399246
MORF4L1Q9UBU8-23EBI-717422,EBI-10288852
MRPL11Q9Y3B73EBI-717422,EBI-5453723
MRPL40Q9NQ503EBI-717422,EBI-1053902
NABP1Q96AH03EBI-717422,EBI-2889252
NPEPL1Q8NDH3-43EBI-717422,EBI-10269715
PHF1O431894EBI-717422,EBI-530034
PITPNM1O005623EBI-717422,EBI-2861268
PLCB1Q9NQ663EBI-717422,EBI-3396023
POLLQ9UGP5-23EBI-717422,EBI-10320765
POLR3GLQ9BT433EBI-717422,EBI-2855862
PPIGQ134273EBI-717422,EBI-396072
PPP1R1BQ9UD713EBI-717422,EBI-722119
PPP3R2Q96LZ33EBI-717422,EBI-3906025
PSMD5Q164013EBI-717422,EBI-752143
RBMS1P295583EBI-717422,EBI-5462600
SDCBPO005603EBI-717422,EBI-727004
STMN2Q930453EBI-717422,EBI-714194
SUMO1P631653EBI-717422,EBI-80140
TCEA2Q155603EBI-717422,EBI-710310
TDRD1Q9BXT4-23EBI-717422,EBI-10301451
TSPAN12O958593EBI-717422,EBI-2466403
ZCCHC10Q8TBK63EBI-717422,EBI-597063
ZCCHC12Q6PEW13EBI-717422,EBI-748373

Protein-protein interaction databases

BioGridi112882. 72 interactions.
IntActiQ12800. 85 interactions.
MINTiMINT-1388673.
STRINGi9606.ENSP00000257915.

Structurei

3D structure databases

ProteinModelPortaliQ12800.
SMRiQ12800. Positions 321-381.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 395263DNA-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi314 – 3196Poly-Pro
Compositional biasi396 – 41318Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the grh/CP2 family. CP2 subfamily.Curated

Phylogenomic databases

eggNOGiNOG275458.
GeneTreeiENSGT00760000119235.
HOGENOMiHOG000230625.
HOVERGENiHBG053805.
InParanoidiQ12800.
KOiK09275.
OMAiDEVCFVL.
OrthoDBiEOG7FBRHB.
PhylomeDBiQ12800.
TreeFamiTF314132.

Family and domain databases

InterProiIPR007604. CP2.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF04516. CP2. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q12800-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAWALKLPLA DEVIESGLVQ DFDASLSGIG QELGAGAYSM SDVLALPIFK
60 70 80 90 100
QEESSLPPDN ENKILPFQYV LCAATSPAVK LHDETLTYLN QGQSYEIRML
110 120 130 140 150
DNRKLGELPE INGKLVKSIF RVVFHDRRLQ YTEHQQLEGW RWNRPGDRIL
160 170 180 190 200
DIDIPMSVGI IDPRANPTQL NTVEFLWDPA KRTSVFIQVH CISTEFTMRK
210 220 230 240 250
HGGEKGVPFR VQIDTFKENE NGEYTEHLHS ASCQIKVFKP KGADRKQKTD
260 270 280 290 300
REKMEKRTPH EKEKYQPSYE TTILTECSPW PEITYVNNSP SPGFNSSHSS
310 320 330 340 350
FSLGEGNGSP NHQPEPPPPV TDNLLPTTTP QEAQQWLHRN RFSTFTRLFT
360 370 380 390 400
NFSGADLLKL TRDDVIQICG PADGIRLFNA LKGRMVRPRL TIYVCQESLQ
410 420 430 440 450
LREQQQQQQQ QQQKHEDGDS NGTFFVYHAI YLEELTAVEL TEKIAQLFSI
460 470 480 490 500
SPCQISQIYK QGPTGIHVLI SDEMIQNFQE EACFILDTMK AETNDSYHII

LK
Length:502
Mass (Da):57,256
Last modified:March 21, 2006 - v2
Checksum:iB93825C2687F89FF
GO
Isoform 2 (identifier: Q12800-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     189-239: Missing.
     491-491: Missing.

Show »
Length:450
Mass (Da):51,308
Checksum:i5004E9DF3925E852
GO
Isoform 3 (identifier: Q12800-3) [UniParc]FASTAAdd to basket

Also known as: LBP-1d

The sequence of this isoform differs from the canonical sequence as follows:
     189-239: Missing.

Show »
Length:451
Mass (Da):51,379
Checksum:i04DAF489CA939B17
GO
Isoform 4 (identifier: Q12800-4) [UniParc]FASTAAdd to basket

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

Show »
Length:501
Mass (Da):57,185
Checksum:i22D5A27DD537009D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921G → A in M84810 (PubMed:1732747).Curated
Sequence conflicti92 – 921G → A AA sequence (PubMed:1732747).Curated
Sequence conflicti249 – 2491T → M in M84810 (PubMed:1732747).Curated
Sequence conflicti249 – 2491T → M AA sequence (PubMed:1732747).Curated
Sequence conflicti491 – 4911A → Q in AAA21324 (PubMed:8035790).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei189 – 23951Missing in isoform 2 and isoform 3. 2 PublicationsVSP_017647Add
BLAST
Alternative sequencei491 – 4911Missing in isoform 2 and isoform 4. 3 PublicationsVSP_017648

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS55827.1. [Q12800-2]
CCDS8808.1. [Q12800-1]
PIRiA42030.
A53771.
C56205.
RefSeqiNP_001166923.1. NM_001173452.1. [Q12800-4]
NP_001166924.1. NM_001173453.1. [Q12800-2]
NP_005644.2. NM_005653.4. [Q12800-1]
UniGeneiHs.48849.

Genome annotation databases

EnsembliENST00000257915; ENSP00000257915; ENSG00000135457. [Q12800-1]
ENST00000548115; ENSP00000447991; ENSG00000135457. [Q12800-2]
GeneIDi7024.
KEGGihsa:7024.
UCSCiuc001rxv.2. human. [Q12800-4]
uc001rxw.3. human. [Q12800-1]
uc009zlx.2. human. [Q12800-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS55827.1. [Q12800-2]
CCDS8808.1. [Q12800-1]
PIRiA42030.
A53771.
C56205.
RefSeqiNP_001166923.1. NM_001173452.1. [Q12800-4]
NP_001166924.1. NM_001173453.1. [Q12800-2]
NP_005644.2. NM_005653.4. [Q12800-1]
UniGeneiHs.48849.

3D structure databases

ProteinModelPortaliQ12800.
SMRiQ12800. Positions 321-381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112882. 72 interactions.
IntActiQ12800. 85 interactions.
MINTiMINT-1388673.
STRINGi9606.ENSP00000257915.

PTM databases

PhosphoSiteiQ12800.

Polymorphism and mutation databases

BioMutaiTFCP2.
DMDMi90101767.

Proteomic databases

MaxQBiQ12800.
PaxDbiQ12800.
PRIDEiQ12800.

Protocols and materials databases

DNASUi7024.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257915; ENSP00000257915; ENSG00000135457. [Q12800-1]
ENST00000548115; ENSP00000447991; ENSG00000135457. [Q12800-2]
GeneIDi7024.
KEGGihsa:7024.
UCSCiuc001rxv.2. human. [Q12800-4]
uc001rxw.3. human. [Q12800-1]
uc009zlx.2. human. [Q12800-2]

Organism-specific databases

CTDi7024.
GeneCardsiGC12M051488.
HGNCiHGNC:11748. TFCP2.
MIMi189889. gene.
neXtProtiNX_Q12800.
PharmGKBiPA36463.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG275458.
GeneTreeiENSGT00760000119235.
HOGENOMiHOG000230625.
HOVERGENiHBG053805.
InParanoidiQ12800.
KOiK09275.
OMAiDEVCFVL.
OrthoDBiEOG7FBRHB.
PhylomeDBiQ12800.
TreeFamiTF314132.

Miscellaneous databases

ChiTaRSiTFCP2. human.
GeneWikiiTFCP2.
GenomeRNAii7024.
NextBioi27443.
PROiQ12800.
SOURCEiSearch...

Gene expression databases

BgeeiQ12800.
CleanExiHS_TFCP2.
ExpressionAtlasiQ12800. baseline and differential.
GenevisibleiQ12800. HS.

Family and domain databases

InterProiIPR007604. CP2.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF04516. CP2. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTFCP2_HUMAN
AccessioniPrimary (citable) accession number: Q12800
Secondary accession number(s): A8K5E9
, Q12801, Q9UD75, Q9UD77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: June 24, 2015
This is version 113 of the entry and version 2 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

Miscellaneous

In PubMed:8114710 authors noted that a 10-fold molar excess of isoform 3 over isoform 1 inhibited DNA-binding.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.