O95365 (ZBT7A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger and BTB domain-containing protein 7A

Alternative name(s):
Factor binding IST protein 1
Short name=FBI-1
Factor that binds to inducer of short transcripts protein 1
HIV-1 1st-binding protein 1
Leukemia/lymphoma-related factor
POZ and Krueppel erythroid myeloid ontogenic factor
Short name=POK erythroid myeloid ontogenic factor
Short name=Pokemon
TTF-I-interacting peptide 21
Short name=TIP21
Zinc finger protein 857A

Gene names

Name:	ZBTB7A
Synonyms:	FBI1, LRF, ZBTB7, ZNF857A

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	584 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a key role in the instruction of early lymphoid progenitors to develop into B lineage by repressing T-cell instructive Notch signals By similarity. Specifically represses the transcription of the CDKN2A gene. Efficiently abrogates E2F1-dependent CDKN2A transactivation/de-repression. Binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' By similarity.
Subunit structure	Interacts with BCL6 By similarity.
Subcellular location	Nucleus By similarity.
Tissue specificity	Widely expressed. In normal thymus, expressed in medullary epithelial cells and Hassle's corpuscles (at protein level). In tonsil, expressed in squamous epithelium and germinal center lymphocytes (at protein level). Up-regulated in a subset of lymphomas, as well as in a subset of breast, lung, colon, prostate and bladder carcinomas (at protein level). Ref.5 Ref.6
Sequence similarities	Contains 1 BTB (POZ) domain. Contains 4 C2H2-type zinc fingers.
Sequence caution	The sequence AAB58414.1 differs from that shown. Reason: Frameshift at positions 8 and 324.

Ontologies

Keywords
Biological process	Differentiation Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Developmental protein Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from sequence or structural similarity PubMed 15337766. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from sequence or structural similarity PubMed 15337766. Source: UniProtKB histone acetyltransferase binding Inferred from sequence or structural similarity PubMed 15337766. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 584

584

Zinc finger and BTB domain-containing protein 7A

PRO_0000047715

Regions

Domain

34 – 101

68

BTB

Zinc finger

382 – 404

23

C2H2-type 1

Zinc finger

410 – 432

23

C2H2-type 2

Zinc finger

438 – 460

23

C2H2-type 3

Zinc finger

466 – 490

25

C2H2-type 4; atypical

Compositional bias

175 – 211

37

Ala-rich

Compositional bias

175 – 181

7

Poly-Ala

Compositional bias

560 – 565

6

Poly-Gly

Amino acid modifications

Modified residue

337

1

Phosphoserine Ref.7 Ref.12

Modified residue

341

1

Phosphoserine Ref.12

Modified residue

495

1

Phosphoserine By similarity

Modified residue

511

1

Phosphoserine Ref.11

Modified residue

525

1

Phosphoserine Ref.11

Modified residue

526

1

Phosphoserine Ref.10

Modified residue

549

1

Phosphoserine Ref.7 Ref.12

Experimental info

Sequence conflict

554

1

G → C in AAH84568. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

584

Helix Strand Turn

Details...

Beta strand

9 – 12

4

Helix

16 – 29

14

Beta strand

36 – 40

5

Beta strand

43 – 47

5

Helix

49 – 55

7

Helix

57 – 64

8

Beta strand

73 – 76

4

Helix

82 – 94

13

Beta strand

95 – 99

5

Helix

101 – 103

3

Helix

104 – 113

10

Helix

117 – 127

11

Sequences

	Sequence		Length	Mass (Da)
	O95365 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 50073663F3D393A0	FASTA	584	61,439
	10 20 30 40 50 60 MAGGVDGPIG IPFPDHSSDI LSGLNEQRTQ GLLCDVVILV EGREFPTHRS VLAACSQYFK 70 80 90 100 110 120 KLFTSGAVVD QQNVYEIDFV SAEALTALMD FAYTATLTVS TANVGDILSA ARLLEIPAVS 130 140 150 160 170 180 HVCADLLDRQ ILAADAGADA GQLDLVDQID QRNLLRAKEY LEFFQSNPMN SLPPAAAAAA 190 200 210 220 230 240 ASFPWSAFGA SDDDLDATKE AVAAAVAAVA AGDCNGLDFY GPGPPAERPP TGDGDEGDSN 250 260 270 280 290 300 PGLWPERDED APTGGLFPPP VAPPAATQNG HYGRGGEEEA ASLSEAAPEP GDSPGFLSGA 310 320 330 340 350 360 AEGEDGDGPD VDGLAASTLL QQMMSSVGRA GAAAGDSDEE SRADDKGVMD YYLKYFSGAH 370 380 390 400 410 420 DGDVYPAWSQ KVEKKIRAKA FQKCPICEKV IQGAGKLPRH IRTHTGEKPY ECNICKVRFT 430 440 450 460 470 480 RQDKLKVHMR KHTGEKPYLC QQCGAAFAHN YDLKNHMRVH TGLRPYQCDS CCKTFVRSDH 490 500 510 520 530 540 LHRHLKKDGC NGVPSRRGRK PRVRGGAPDP SPGATATPGA PAQPSSPDAR RNGQEKHFKD 550 560 570 580 EDEDEDVASP DGLGRLNVAG AGGGGDSGGG PGAATDGNFT AGLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"FBI-1, a factor that binds to the HIV-1 inducer of short transcripts (IST), is a POZ domain protein." Morrison D.J., Pendergrast P.S., Stavropoulos P., Colmenares S.U., Kobayashi R., Hernandez N. Nucleic Acids Res. 27:1251-1262(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Carcinoma.
[2]	"cDNA encoding TTF-I interacting peptide 21 (TIP21)." Jansa P., Grummt I. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Pancreas.
[5]	"Novel BTB/POZ domain zinc-finger protein, LRF, is a potential target of the LAZ-3/BCL-6 oncogene." Davies J.M., Hawe N., Kabarowski J., Huang Q.-H., Zhu J., Brand N.J., Leprince D., Dhordain P., Cook M., Moriss-Kay G., Zelent A. Oncogene 18:365-375(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"Role of the proto-oncogene Pokemon in cellular transformation and ARF repression." Maeda T., Hobbs R.M., Merghoub T., Guernah I., Zelent A., Cordon-Cardo C., Teruya-Feldstein J., Pandolfi P.P. Nature 433:278-285(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-549, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-511 AND SER-525, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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-337; SER-341 AND SER-549, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Structure of the POZ domain of human LRF, a master regulator of oncogenesis." Schubot F.D., Tropea J.E., Waugh D.S. Biochem. Biophys. Res. Commun. 351:1-6(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 9-128.
[14]	"Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulator." Stogios P.J., Chen L., Prive G.G. Protein Sci. 16:336-342(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-131.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF097916 mRNA. Translation: AAC72973.1.
AF000561 mRNA. Translation: AAB58414.1. Frameshift.
CH471139 Genomic DNA. Translation: EAW69267.1.
CH471139 Genomic DNA. Translation: EAW69268.1.
CH471139 Genomic DNA. Translation: EAW69270.1.
CH471139 Genomic DNA. Translation: EAW69271.1.
CH471139 Genomic DNA. Translation: EAW69272.1.
BC084568 mRNA. Translation: AAH84568.1.
BC113511 mRNA. Translation: AAI13512.1.

IPI

IPI00026317.

RefSeq

NP_056982.1. NM_015898.2.

UniGene

Hs.591384.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IF5	X-ray	2.00	A	9-128	[»]
2NN2	X-ray	2.10	A/B	1-131	[»]

ProteinModelPortal

O95365.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95365. 1 interaction.

STRING

9606.ENSP00000323670.

PTM databases

PhosphoSite

O95365.

Proteomic databases

PaxDb

O95365.

PRIDE

O95365.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000322357; ENSP00000323670; ENSG00000178951.
ENST00000601588; ENSP00000471865; ENSG00000178951.

GeneID

51341.

KEGG

hsa:51341.

UCSC

uc002lzh.3. human.

Organism-specific databases

CTD

51341.

GeneCards

GC19M004045.

HGNC

HGNC:18078. ZBTB7A.

HPA

CAB037214.

MIM

605878. gene.

neXtProt

NX_O95365.

PharmGKB

PA134885165.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5048.

HOGENOM

HOG000082521.

HOVERGEN

HBG106747.

InParanoid

O95365.

KO

K10494.

OMA

HEGDVYP.

OrthoDB

EOG4DZ1X1.

PhylomeDB

O95365.

Gene expression databases

Bgee

O95365.

CleanEx

HS_ZBTB7A.

Genevestigator

O95365.

GermOnline

ENSG00000178951. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.60. 4 hits.
3.30.710.10. 1 hit.

InterPro

IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Pfam

PF00651. BTB. 1 hit.
[Graphical view]

SMART

SM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 4 hits.
[Graphical view]

SUPFAM

SSF54695. BTB/POZ_fold. 1 hit.

PROSITE

PS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ZBTB7A. human.

EvolutionaryTrace

O95365.

GenomeRNAi

51341.

NextBio

54786.

SOURCE

Search...

Entry information

Entry name

ZBT7A_HUMAN

Accession

Primary (citable) accession number: O95365
Secondary accession number(s): D6W619 , O00456, Q14D41, Q5XG86

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 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.