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Q13105 (ZBT17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length803 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. 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. 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 Ref.13

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. 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. Interacts with BCL6; the interaction inhibits ZBTB17 transactivation activity on target genes involved in cell cycle arrest. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15

Subcellular location

Nucleus Ref.1 Ref.10.

Tissue specificity

Expressed in germinal center B-cells. Ref.12

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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionDevelopmental protein
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

ectoderm development

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

gastrulation with mouth forming second

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell cycle

Traceable author statement Ref.8. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.8Ref.7. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 803803Zinc finger and BTB domain-containing protein 17
PRO_0000047730

Regions

Domain1 – 104104BTB
Zinc finger306 – 32823C2H2-type 1
Zinc finger334 – 35623C2H2-type 2
Zinc finger362 – 38423C2H2-type 3
Zinc finger390 – 41223C2H2-type 4
Zinc finger418 – 44023C2H2-type 5
Zinc finger446 – 46823C2H2-type 6
Zinc finger474 – 49623C2H2-type 7
Zinc finger502 – 52423C2H2-type 8
Zinc finger530 – 55223C2H2-type 9
Zinc finger558 – 58023C2H2-type 10
Zinc finger586 – 60823C2H2-type 11
Zinc finger614 – 63724C2H2-type 12
Zinc finger717 – 73923C2H2-type 13
Region269 – 30840Interaction with MYC
Region637 – 803167Interaction with HCFC1
Region637 – 71882Interaction with MYC

Amino acid modifications

Cross-link397Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence1 – 131131MDFPQ…ALATE → MMCWPWPLSSKCRTSSRPAM PSSHLLSRLPALGEMRRPWP QKVCPVPSP in isoform 3.
VSP_044564
Alternative sequence6791T → TGPATLPA in isoform 2.
VSP_013424

Experimental info

Sequence conflict731V → M in CAA70889. Ref.1
Sequence conflict3341F → S in BAG63326. Ref.2

Secondary structure

.................................................. 803
Helix Strand Turn

Details...

Sequences

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

Last modified April 26, 2005. Version 3.
Checksum: C159D177C8A2D4A3

FASTA80387,928
        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 

« Hide

Isoform 2 [UniParc].

Checksum: E59D5EBF4A77C210
Show »

FASTA81088,535
Isoform 3 [UniParc].

Checksum: 7C8788248C093F0D
Show »

FASTA72179,228

References

« Hide '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. 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 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. expand/collapse author list , 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]"BCL6 interacts with the transcription factor Miz-1 to suppress the cyclin-dependent kinase inhibitor p21 and cell cycle arrest in germinal center B cells."
Phan R.T., Saito M., Basso K., Niu H., Dalla-Favera R.
Nat. Immunol. 6:1054-1060(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL CYCLE ARREST, INTERACTION WITH BCL6, TISSUE SPECIFICITY.
[13]"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.
[14]"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].
[15]"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.
CCDSCCDS165.1. [Q13105-1]
CCDS55576.1. [Q13105-3]
PIRD45193.
I38940.
RefSeqNP_001229813.1. NM_001242884.1. [Q13105-3]
NP_001274532.1. NM_001287603.1. [Q13105-2]
NP_003434.2. NM_003443.2. [Q13105-1]
UniGeneHs.433764.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LVRNMR-A500-528[»]
2LVTNMR-A528-556[»]
2LVUNMR-A556-581[»]
2M0DNMR-A416-444[»]
2M0ENMR-A444-472[»]
2M0FNMR-A472-500[»]
2Q81X-ray2.10A/B/C/D2-115[»]
3M52X-ray2.59A/B1-115[»]
ProteinModelPortalQ13105.
SMRQ13105. Positions 1-115, 303-776.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113503. 18 interactions.
DIPDIP-5968N.
IntActQ13105. 9 interactions.
MINTMINT-1527698.
STRING9606.ENSP00000364895.

PTM databases

PhosphoSiteQ13105.

Polymorphism databases

DMDM62906906.

Proteomic databases

MaxQBQ13105.
PaxDbQ13105.
PRIDEQ13105.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375733; ENSP00000364885; ENSG00000116809. [Q13105-2]
ENST00000375743; ENSP00000364895; ENSG00000116809. [Q13105-1]
ENST00000537142; ENSP00000438529; ENSG00000116809. [Q13105-3]
GeneID7709.
KEGGhsa:7709.
UCSCuc001axl.4. human. [Q13105-1]
uc010obr.2. human. [Q13105-2]

Organism-specific databases

CTD7709.
GeneCardsGC01M016268.
HGNCHGNC:12936. ZBTB17.
HPAHPA005789.
MIM604084. gene.
neXtProtNX_Q13105.
PharmGKBPA37522.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000231298.
HOVERGENHBG054919.
KOK10500.
OMACDSCGDK.
OrthoDBEOG7KSX7Q.
PhylomeDBQ13105.
TreeFamTF332047.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ13105.
BgeeQ13105.
CleanExHS_ZBTB17.
GenevestigatorQ13105.

Family and domain databases

Gene3D3.30.160.60. 13 hits.
3.30.710.10. 1 hit.
InterProIPR000210. 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]
PfamPF00651. BTB. 1 hit.
[Graphical view]
SMARTSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 13 hits.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 13 hits.
PS50157. ZINC_FINGER_C2H2_2. 13 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZBTB17. human.
EvolutionaryTraceQ13105.
GeneWikiZBTB17.
GenomeRNAi7709.
NextBio29884.
PROQ13105.
SOURCESearch...

Entry information

Entry nameZBT17_HUMAN
AccessionPrimary (citable) accession number: Q13105
Secondary accession number(s): A0AV07 expand/collapse secondary AC list , B4DXB4, B7ZLQ9, F5H411, Q15932, Q5JYB2, Q9NUC9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 26, 2005
Last modified: July 9, 2014
This is version 151 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM