Q13105 (ZBT17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger and BTB domain-containing protein 17

Alternative name(s):
Myc-interacting zinc finger protein 1
Short name=Miz-1
Zinc finger protein 151
Zinc finger protein 60

Gene names

Name:	ZBTB17
Synonyms:	MIZ1, ZNF151, ZNF60

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

General annotation (Comments)

Function	Plays a critical role in early lymphocyte development, where it is essential to prevent apoptosis in lymphoid precursors, allowing them to survive in response to IL7 and undergo proper lineage commitment By similarity. Transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. Has been shown to bind to the promoters of adenovirus major late protein and cyclin D1 and activate transcription. Required for early embryonic development during gastrulation. Ref.1 Ref.7 Ref.12
Subunit structure	Homooligomerizes (via the BTB/POZ domain), multimerization is required for DNA binding. Interacts (via the C-terminal zinc fingers) with GIF1; the interaction results in the recruitment of MYB to the CDKN1A/p21 and CDKN1B promoters and repression of transcription. Interacts with TRAF2, interfering with the binding of UBC13 to TRAF2, and inhibiting TRAF2 E3 ligase activity By similarity. Interacts with MYC (via the C-terminal helix-loop-helix motif): the interaction inhibits ZBTB17 transactivation and growth arrest activities and renders it insoluble in the nucleus. Also interacts with HCFC1, MAGEA4 and TMPRSS11A. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14
Subcellular location	Nucleus Ref.1 Ref.10.
Post-translational modification	Undergoes 'Lys-48'-linked polyubiquitination at Lys-397 and Lys-481 and subsequent proteasomal degradation in a TRAF2-dependent manner By similarity.
Sequence similarities	Belongs to the krueppel C2H2-type zinc-finger protein family. Contains 1 BTB (POZ) domain. Contains 13 C2H2-type zinc fingers.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Developmental protein
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome ectoderm development Inferred from electronic annotation. Source: Compara gastrulation with mouth forming second Inferred from electronic annotation. Source: Compara negative regulation of cell cycle Traceable author statement Ref.8. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Inferred from direct assay Ref.8. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HCFC1	P51610	9	EBI-372156,EBI-396176
MAGEA4	P43358	5	EBI-372156,EBI-743122
MYC	P01106	2	EBI-372156,EBI-447544

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13105-1)

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: Q13105-2)

The sequence of this isoform differs from the canonical sequence as follows:
     679-679: T → TGPATLPA

Note: No experimental confirmation available.

Isoform 3 (identifier: Q13105-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: MDFPQHSQHV...GGNAEALATE → MMCWPWPLSS...PQKVCPVPSP

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 803

803

Zinc finger and BTB domain-containing protein 17

PRO_0000047730

Regions

Domain

1 – 104

104

BTB

Zinc finger

306 – 328

23

C2H2-type 1

Zinc finger

334 – 356

23

C2H2-type 2

Zinc finger

362 – 384

23

C2H2-type 3

Zinc finger

390 – 412

23

C2H2-type 4

Zinc finger

418 – 440

23

C2H2-type 5

Zinc finger

446 – 468

23

C2H2-type 6

Zinc finger

474 – 496

23

C2H2-type 7

Zinc finger

502 – 524

23

C2H2-type 8

Zinc finger

530 – 552

23

C2H2-type 9

Zinc finger

558 – 580

23

C2H2-type 10

Zinc finger

586 – 608

23

C2H2-type 11

Zinc finger

614 – 637

24

C2H2-type 12

Zinc finger

717 – 739

23

C2H2-type 13

Region

269 – 308

40

Interaction with MYC

Region

637 – 803

167

Interaction with HCFC1

Region

637 – 718

82

Interaction with MYC

Amino acid modifications

Cross-link

397

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

481

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence

1 – 131

131

MDFPQ…ALATE → MMCWPWPLSSKCRTSSRPAM PSSHLLSRLPALGEMRRPWP QKVCPVPSP in isoform 3.

VSP_044564

Alternative sequence

679

1

T → TGPATLPA in isoform 2.

VSP_013424

Experimental info

Sequence conflict

73

1

V → M in CAA70889. Ref.1

Sequence conflict

334

1

F → S in BAG63326. Ref.2

Secondary structure

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803

Helix Strand Turn

Details...

Helix

3 – 20

18

Beta strand

26 – 30

5

Beta strand

33 – 37

5

Helix

39 – 45

7

Helix

47 – 55

9

Helix

56 – 58

3

Helix

59 – 64

6

Helix

67 – 79

13

Turn

86 – 88

3

Helix

89 – 98

10

Helix

102 – 112

11

Turn

421 – 423

3

Beta strand

426 – 428

3

Helix

430 – 438

9

Turn

457 – 459

3

Helix

460 – 469

10

Turn

477 – 479

3

Beta strand

482 – 484

3

Helix

486 – 497

12

Turn

505 – 507

3

Beta strand

510 – 512

3

Helix

514 – 525

12

Turn

533 – 535

3

Beta strand

538 – 541

4

Helix

542 – 553

12

Turn

561 – 563

3

Helix

570 – 578

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 26, 2005. Version 3. Checksum: C159D177C8A2D4A3	FASTA	803	87,928
	10 20 30 40 50 60 MDFPQHSQHV LEQLNQQRQL GLLCDCTFVV DGVHFKAHKA VLAACSEYFK MLFVDQKDVV 70 80 90 100 110 120 HLDISNAAGL GQVLEFMYTA KLSLSPENVD DVLAVATFLQ MQDIITACHA LKSLAEPATS 130 140 150 160 170 180 PGGNAEALAT EGGDKRAKEE KVATSTLSRL EQAGRSTPIG PSRDLKEERG GQAQSAASGA 190 200 210 220 230 240 EQTEKADAPR EPPPVELKPD PTSGMAAAEA EAALSESSEQ EMEVEPARKG EEEQKEQEEQ 250 260 270 280 290 300 EEEGAGPAEV KEEGSQLENG EAPEENENEE SAGTDSGQEL GSEARGLRSG TYGDRTESKA 310 320 330 340 350 360 YGSVIHKCED CGKEFTHTGN FKRHIRIHTG EKPFSCRECS KAFSDPAACK AHEKTHSPLK 370 380 390 400 410 420 PYGCEECGKS YRLISLLNLH KKRHSGEARY RCEDCGKLFT TSGNLKRHQL VHSGEKPYQC 430 440 450 460 470 480 DYCGRSFSDP TSKMRHLETH DTDKEHKCPH CDKKFNQVGN LKAHLKIHIA DGPLKCRECG 490 500 510 520 530 540 KQFTTSGNLK RHLRIHSGEK PYVCIHCQRQ FADPGALQRH VRIHTGEKPC QCVMCGKAFT 550 560 570 580 590 600 QASSLIAHVR QHTGEKPYVC ERCGKRFVQS SQLANHIRHH DNIRPHKCSV CSKAFVNVGD 610 620 630 640 650 660 LSKHIIIHTG EKPYLCDKCG RGFNRVDNLR SHVKTVHQGK AGIKILEPEE GSEVSVVTVD 670 680 690 700 710 720 DMVTLATEAL AATAVTQLTV VPVGAAVTAD ETEVLKAEIS KAVKQVQEED PNTHILYACD 730 740 750 760 770 780 SCGDKFLDAN SLAQHVRIHT AQALVMFQTD ADFYQQYGPG GTWPAGQVLQ AGELVFRPRD 790 800 GAEGQPALAE TSPTAPECPP PAE
	Isoform 2 [UniParc]. Checksum: E59D5EBF4A77C210	FASTA	810	88,535
	10 20 30 40 50 60 MDFPQHSQHV LEQLNQQRQL GLLCDCTFVV DGVHFKAHKA VLAACSEYFK MLFVDQKDVV 70 80 90 100 110 120 HLDISNAAGL GQVLEFMYTA KLSLSPENVD DVLAVATFLQ MQDIITACHA LKSLAEPATS 130 140 150 160 170 180 PGGNAEALAT EGGDKRAKEE KVATSTLSRL EQAGRSTPIG PSRDLKEERG GQAQSAASGA 190 200 210 220 230 240 EQTEKADAPR EPPPVELKPD PTSGMAAAEA EAALSESSEQ EMEVEPARKG EEEQKEQEEQ 250 260 270 280 290 300 EEEGAGPAEV KEEGSQLENG EAPEENENEE SAGTDSGQEL GSEARGLRSG TYGDRTESKA 310 320 330 340 350 360 YGSVIHKCED CGKEFTHTGN FKRHIRIHTG EKPFSCRECS KAFSDPAACK AHEKTHSPLK 370 380 390 400 410 420 PYGCEECGKS YRLISLLNLH KKRHSGEARY RCEDCGKLFT TSGNLKRHQL VHSGEKPYQC 430 440 450 460 470 480 DYCGRSFSDP TSKMRHLETH DTDKEHKCPH CDKKFNQVGN LKAHLKIHIA DGPLKCRECG 490 500 510 520 530 540 KQFTTSGNLK RHLRIHSGEK PYVCIHCQRQ FADPGALQRH VRIHTGEKPC QCVMCGKAFT 550 560 570 580 590 600 QASSLIAHVR QHTGEKPYVC ERCGKRFVQS SQLANHIRHH DNIRPHKCSV CSKAFVNVGD 610 620 630 640 650 660 LSKHIIIHTG EKPYLCDKCG RGFNRVDNLR SHVKTVHQGK AGIKILEPEE GSEVSVVTVD 670 680 690 700 710 720 DMVTLATEAL AATAVTQLTG PATLPAVVPV GAAVTADETE VLKAEISKAV KQVQEEDPNT 730 740 750 760 770 780 HILYACDSCG DKFLDANSLA QHVRIHTAQA LVMFQTDADF YQQYGPGGTW PAGQVLQAGE 790 800 810 LVFRPRDGAE GQPALAETSP TAPECPPPAE
	Isoform 3 [UniParc]. Checksum: 7C8788248C093F0D	FASTA	721	79,228
	10 20 30 40 50 60 MMCWPWPLSS KCRTSSRPAM PSSHLLSRLP ALGEMRRPWP QKVCPVPSPG GDKRAKEEKV 70 80 90 100 110 120 ATSTLSRLEQ AGRSTPIGPS RDLKEERGGQ AQSAASGAEQ TEKADAPREP PPVELKPDPT 130 140 150 160 170 180 SGMAAAEAEA ALSESSEQEM EVEPARKGEE EQKEQEEQEE EGAGPAEVKE EGSQLENGEA 190 200 210 220 230 240 PEENENEESA GTDSGQELGS EARGLRSGTY GDRTESKAYG SVIHKCEDCG KEFTHTGNFK 250 260 270 280 290 300 RHIRIHTGEK PFSCRECSKA FSDPAACKAH EKTHSPLKPY GCEECGKSYR LISLLNLHKK 310 320 330 340 350 360 RHSGEARYRC EDCGKLFTTS GNLKRHQLVH SGEKPYQCDY CGRSFSDPTS KMRHLETHDT 370 380 390 400 410 420 DKEHKCPHCD KKFNQVGNLK AHLKIHIADG PLKCRECGKQ FTTSGNLKRH LRIHSGEKPY 430 440 450 460 470 480 VCIHCQRQFA DPGALQRHVR IHTGEKPCQC VMCGKAFTQA SSLIAHVRQH TGEKPYVCER 490 500 510 520 530 540 CGKRFVQSSQ LANHIRHHDN IRPHKCSVCS KAFVNVGDLS KHIIIHTGEK PYLCDKCGRG 550 560 570 580 590 600 FNRVDNLRSH VKTVHQGKAG IKILEPEEGS EVSVVTVDDM VTLATEALAA TAVTQLTVVP 610 620 630 640 650 660 VGAAVTADET EVLKAEISKA VKQVQEEDPN THILYACDSC GDKFLDANSL AQHVRIHTAQ 670 680 690 700 710 720 ALVMFQTDAD FYQQYGPGGT WPAGQVLQAG ELVFRPRDGA EGQPALAETS PTAPECPPPA E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An alternative pathway for gene regulation by Myc." Peukert K., Staller P., Schneider A., Carmichael G., Haenel F., Eilers M. EMBO J. 16:5672-5686(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYC.
[2]	"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 3). Tissue: Testis.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] 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] (ISOFORMS 1 AND 2). Tissue: Brain.
[5]	"Clustering of C2-H2 zinc finger motif sequences within telomeric and fragile site regions of human chromosomes." Lichter P., Bray P., Ried T., Dawid I.B., Ward D.C. Genomics 13:999-1007(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 327-342. Tissue: Placenta.
[6]	"Isolation and fine mapping of 16 novel human zinc finger-encoding cDNAs identify putative candidate genes for developmental and malignant disorders." Tommerup N., Vissing H. Genomics 27:259-264(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 580-803 (ISOFORM 1). Tissue: Insulinoma.
[7]	"Association of Myc with the zinc-finger protein Miz-1 defines a novel pathway for gene regulation by Myc." Schneider A., Peukert K., Eilers M., Haenel F. Curr. Top. Microbiol. Immunol. 224:137-146(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Tissue: Cervix carcinoma.
[8]	"Host cell factor-1 interacts with and antagonizes transactivation by the cell cycle regulatory factor Miz-1." Piluso D., Bilan P., Capone J.P. J. Biol. Chem. 277:46799-46808(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HCFC1.
[9]	"Myc represses differentiation-induced p21CIP1 expression via Miz-1-dependent interaction with the p21 core promoter." Wu S., Cetinkaya C., Munoz-Alonso M.J., von der Lehr N., Bahram F., Beuger V., Eilers M., Leon J., Larsson L.-G. Oncogene 22:351-360(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYC.
[10]	"A cleaved form of MAGE-A4 binds to Miz-1 and induces apoptosis in human cells." Sakurai T., Itoh K., Higashitsuji H., Nagao T., Nonoguchi K., Chiba T., Fujita J. J. Biol. Chem. 279:15505-15514(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAGEA4, SUBCELLULAR LOCATION.
[11]	"Induction of G1 cell cycle arrest and P15INK4b expression by ECRG1 through interaction with Miz-1." Zhao N., Wang J., Cui Y., Guo L., Lu S.-H. J. Cell. Biochem. 92:65-76(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TMPRSS11A.
[12]	"Gfi-1 represses CDKN2B encoding p15INK4B through interaction with Miz-1." Basu S., Liu Q., Qiu Y., Dong F. Proc. Natl. Acad. Sci. U.S.A. 106:1433-1438(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"A beta-sheet interaction interface directs the tetramerisation of the Miz-1 POZ domain." Stead M.A., Trinh C.H., Garnett J.A., Carr S.B., Baron A.J., Edwards T.A., Wright S.C. J. Mol. Biol. 373:820-826(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-115, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y09723 mRNA. Translation: CAA70889.1.
AK301896 mRNA. Translation: BAG63326.1.
AL034555 Genomic DNA. Translation: CAB85445.1.
AL034555 Genomic DNA. Translation: CAI19524.1.
AL355994 Genomic DNA. No translation available.
BC126163 mRNA. Translation: AAI26164.1.
BC143965 mRNA. Translation: AAI43966.1.
M88369 Genomic DNA. Translation: AAA61327.1.
U20647 mRNA. Translation: AAC50256.1.

IPI

IPI00011834.
IPI00556634.
IPI01009418.

PIR

D45193.
I38940.

RefSeq

NP_001229813.1. NM_001242884.1.
NP_003434.2. NM_003443.2.

UniGene

Hs.433764.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LVR	NMR	-	A	500-528	[»]
2LVT	NMR	-	A	528-556	[»]
2LVU	NMR	-	A	556-581	[»]
2M0D	NMR	-	A	416-444	[»]
2M0E	NMR	-	A	444-472	[»]
2M0F	NMR	-	A	472-500	[»]
2Q81	X-ray	2.10	A/B/C/D	2-115	[»]
3M52	X-ray	2.59	A/B	1-115	[»]

ProteinModelPortal

Q13105.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5968N.

IntAct

Q13105. 7 interactions.

STRING

9606.ENSP00000364895.

PTM databases

PhosphoSite

Q13105.

Polymorphism databases

DMDM

62906906.

Proteomic databases

PaxDb

Q13105.

PRIDE

Q13105.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375733; ENSP00000364885; ENSG00000116809.
ENST00000375743; ENSP00000364895; ENSG00000116809.
ENST00000537142; ENSP00000438529; ENSG00000116809.

GeneID

7709.

KEGG

hsa:7709.

UCSC

uc001axl.4. human.
uc010obr.2. human.

Organism-specific databases

CTD

7709.

GeneCards

GC01M016268.

HGNC

HGNC:12936. ZBTB17.

HPA

HPA005789.

MIM

604084. gene.

neXtProt

NX_Q13105.

PharmGKB

PA37522.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5048.

HOGENOM

HOG000231298.

HOVERGEN

HBG054919.

KO

K10500.

OMA

CDSCGDK.

OrthoDB

EOG4GHZNQ.

PhylomeDB

Q13105.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q13105.

Bgee

Q13105.

CleanEx

HS_ZBTB17.

Genevestigator

Q13105.

GermOnline

ENSG00000116809. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.60. 13 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. 13 hits.
[Graphical view]

SUPFAM

SSF54695. BTB/POZ_fold. 1 hit.

PROSITE

PS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 13 hits.
PS50157. ZINC_FINGER_C2H2_2. 13 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ZBTB17. human.

EvolutionaryTrace

Q13105.

GenomeRNAi

7709.

NextBio

29884.

SOURCE

Search...

Entry information

Entry name

ZBT17_HUMAN

Accession

Primary (citable) accession number: Q13105
Secondary accession number(s): A0AV07 , B4DXB4, B7ZLQ9, F5H411, Q15932, Q5JYB2, Q9NUC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	April 26, 2005
Last modified:	May 1, 2013
This is version 139 of the entry and version 3 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.