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Q13105

- ZBT17_HUMAN

UniProt

Q13105 - ZBT17_HUMAN

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Protein

Zinc finger and BTB domain-containing protein 17

Gene

ZBTB17

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

Functioni

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.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri306 – 32823C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri334 – 35623C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri362 – 38423C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri390 – 41223C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri418 – 44023C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri446 – 46823C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri474 – 49623C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri502 – 52423C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri530 – 55223C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri558 – 58023C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri586 – 60823C2H2-type 11PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri614 – 63724C2H2-type 12PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri717 – 73923C2H2-type 13PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. ectoderm development Source: Ensembl
  4. endoplasmic reticulum unfolded protein response Source: Reactome
  5. gastrulation with mouth forming second Source: Ensembl
  6. negative regulation of cell cycle Source: UniProtKB
  7. positive regulation of transcription, DNA-templated Source: Ensembl
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ZBTB17
Synonyms:MIZ1, ZNF151, ZNF60
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:12936. ZBTB17.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37522.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 803803Zinc finger and BTB domain-containing protein 17PRO_0000047730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki397 – 397Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki481 – 481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Undergoes 'Lys-48'-linked polyubiquitination at Lys-397 and Lys-481 and subsequent proteasomal degradation in a TRAF2-dependent manner.By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ13105.
PaxDbiQ13105.
PRIDEiQ13105.

PTM databases

PhosphoSiteiQ13105.

Expressioni

Tissue specificityi

Expressed in germinal center B-cells.1 Publication

Gene expression databases

BgeeiQ13105.
CleanExiHS_ZBTB17.
GenevestigatoriQ13105.

Organism-specific databases

HPAiHPA005789.

Interactioni

Subunit structurei

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HCFC1P516109EBI-372156,EBI-396176
MAGEA4P433585EBI-372156,EBI-743122
MYCP011064EBI-372156,EBI-447544
TOPBP1Q925472EBI-372156,EBI-308302

Protein-protein interaction databases

BioGridi113503. 18 interactions.
DIPiDIP-5968N.
IntActiQ13105. 9 interactions.
MINTiMINT-1527698.
STRINGi9606.ENSP00000364895.

Structurei

Secondary structure

1
803
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2018
Beta strandi26 – 305
Beta strandi33 – 375
Helixi39 – 457
Helixi47 – 559
Helixi56 – 583
Helixi59 – 646
Helixi67 – 7913
Turni86 – 883
Helixi89 – 9810
Helixi102 – 11211
Turni421 – 4233
Beta strandi426 – 4283
Helixi430 – 4389
Turni457 – 4593
Helixi460 – 46910
Turni477 – 4793
Beta strandi482 – 4843
Helixi486 – 49712
Turni505 – 5073
Beta strandi510 – 5123
Helixi514 – 52512
Turni533 – 5353
Beta strandi538 – 5414
Helixi542 – 55312
Turni561 – 5633
Helixi570 – 5789

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ13105.
SMRiQ13105. Positions 1-115, 306-635, 717-744.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13105.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 104104BTBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni269 – 30840Interaction with MYCAdd
BLAST
Regioni637 – 803167Interaction with HCFC1Add
BLAST
Regioni637 – 71882Interaction with MYCAdd
BLAST

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 13 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri306 – 32823C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri334 – 35623C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri362 – 38423C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri390 – 41223C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri418 – 44023C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri446 – 46823C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri474 – 49623C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri502 – 52423C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri530 – 55223C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri558 – 58023C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri586 – 60823C2H2-type 11PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri614 – 63724C2H2-type 12PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri717 – 73923C2H2-type 13PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118922.
HOGENOMiHOG000231298.
HOVERGENiHBG054919.
InParanoidiQ13105.
KOiK10500.
OMAiCDSCGDK.
OrthoDBiEOG7KSX7Q.
PhylomeDBiQ13105.
TreeFamiTF332047.

Family and domain databases

Gene3Di3.30.160.60. 13 hits.
3.30.710.10. 1 hit.
InterProiIPR000210. 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]
PfamiPF00651. BTB. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 13 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 13 hits.
PS50157. ZINC_FINGER_C2H2_2. 13 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13105) [UniParc]FASTAAdd to Basket

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
MDFPQHSQHV LEQLNQQRQL GLLCDCTFVV DGVHFKAHKA VLAACSEYFK
60 70 80 90 100
MLFVDQKDVV HLDISNAAGL GQVLEFMYTA KLSLSPENVD DVLAVATFLQ
110 120 130 140 150
MQDIITACHA LKSLAEPATS PGGNAEALAT EGGDKRAKEE KVATSTLSRL
160 170 180 190 200
EQAGRSTPIG PSRDLKEERG GQAQSAASGA EQTEKADAPR EPPPVELKPD
210 220 230 240 250
PTSGMAAAEA EAALSESSEQ EMEVEPARKG EEEQKEQEEQ EEEGAGPAEV
260 270 280 290 300
KEEGSQLENG EAPEENENEE SAGTDSGQEL GSEARGLRSG TYGDRTESKA
310 320 330 340 350
YGSVIHKCED CGKEFTHTGN FKRHIRIHTG EKPFSCRECS KAFSDPAACK
360 370 380 390 400
AHEKTHSPLK PYGCEECGKS YRLISLLNLH KKRHSGEARY RCEDCGKLFT
410 420 430 440 450
TSGNLKRHQL VHSGEKPYQC DYCGRSFSDP TSKMRHLETH DTDKEHKCPH
460 470 480 490 500
CDKKFNQVGN LKAHLKIHIA DGPLKCRECG KQFTTSGNLK RHLRIHSGEK
510 520 530 540 550
PYVCIHCQRQ FADPGALQRH VRIHTGEKPC QCVMCGKAFT QASSLIAHVR
560 570 580 590 600
QHTGEKPYVC ERCGKRFVQS SQLANHIRHH DNIRPHKCSV CSKAFVNVGD
610 620 630 640 650
LSKHIIIHTG EKPYLCDKCG RGFNRVDNLR SHVKTVHQGK AGIKILEPEE
660 670 680 690 700
GSEVSVVTVD DMVTLATEAL AATAVTQLTV VPVGAAVTAD ETEVLKAEIS
710 720 730 740 750
KAVKQVQEED PNTHILYACD SCGDKFLDAN SLAQHVRIHT AQALVMFQTD
760 770 780 790 800
ADFYQQYGPG GTWPAGQVLQ AGELVFRPRD GAEGQPALAE TSPTAPECPP

PAE
Length:803
Mass (Da):87,928
Last modified:April 26, 2005 - v3
Checksum:iC159D177C8A2D4A3
GO
Isoform 2 (identifier: Q13105-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:810
Mass (Da):88,535
Checksum:iE59D5EBF4A77C210
GO
Isoform 3 (identifier: Q13105-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:721
Mass (Da):79,228
Checksum:i7C8788248C093F0D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731V → M in CAA70889. (PubMed:9312026)Curated
Sequence conflicti334 – 3341F → S in BAG63326. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 131131MDFPQ…ALATE → MMCWPWPLSSKCRTSSRPAM PSSHLLSRLPALGEMRRPWP QKVCPVPSP in isoform 3. 1 PublicationVSP_044564Add
BLAST
Alternative sequencei679 – 6791T → TGPATLPA in isoform 2. 1 PublicationVSP_013424

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS165.1. [Q13105-1]
CCDS55576.1. [Q13105-3]
CCDS72712.1. [Q13105-2]
PIRiD45193.
I38940.
RefSeqiNP_001229813.1. NM_001242884.1. [Q13105-3]
NP_001274532.1. NM_001287603.1. [Q13105-2]
NP_003434.2. NM_003443.2. [Q13105-1]
UniGeneiHs.433764.

Genome annotation databases

EnsembliENST00000375733; ENSP00000364885; ENSG00000116809. [Q13105-2]
ENST00000375743; ENSP00000364895; ENSG00000116809. [Q13105-1]
ENST00000537142; ENSP00000438529; ENSG00000116809. [Q13105-3]
GeneIDi7709.
KEGGihsa:7709.
UCSCiuc001axl.4. human. [Q13105-1]
uc010obr.2. human. [Q13105-2]

Polymorphism databases

DMDMi62906906.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS165.1. [Q13105-1 ]
CCDS55576.1. [Q13105-3 ]
CCDS72712.1. [Q13105-2 ]
PIRi D45193.
I38940.
RefSeqi NP_001229813.1. NM_001242884.1. [Q13105-3 ]
NP_001274532.1. NM_001287603.1. [Q13105-2 ]
NP_003434.2. NM_003443.2. [Q13105-1 ]
UniGenei Hs.433764.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q13105.
SMRi Q13105. Positions 1-115, 306-635, 717-744.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113503. 18 interactions.
DIPi DIP-5968N.
IntActi Q13105. 9 interactions.
MINTi MINT-1527698.
STRINGi 9606.ENSP00000364895.

PTM databases

PhosphoSitei Q13105.

Polymorphism databases

DMDMi 62906906.

Proteomic databases

MaxQBi Q13105.
PaxDbi Q13105.
PRIDEi Q13105.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375733 ; ENSP00000364885 ; ENSG00000116809 . [Q13105-2 ]
ENST00000375743 ; ENSP00000364895 ; ENSG00000116809 . [Q13105-1 ]
ENST00000537142 ; ENSP00000438529 ; ENSG00000116809 . [Q13105-3 ]
GeneIDi 7709.
KEGGi hsa:7709.
UCSCi uc001axl.4. human. [Q13105-1 ]
uc010obr.2. human. [Q13105-2 ]

Organism-specific databases

CTDi 7709.
GeneCardsi GC01M016268.
HGNCi HGNC:12936. ZBTB17.
HPAi HPA005789.
MIMi 604084. gene.
neXtProti NX_Q13105.
PharmGKBi PA37522.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5048.
GeneTreei ENSGT00760000118922.
HOGENOMi HOG000231298.
HOVERGENi HBG054919.
InParanoidi Q13105.
KOi K10500.
OMAi CDSCGDK.
OrthoDBi EOG7KSX7Q.
PhylomeDBi Q13105.
TreeFami TF332047.

Enzyme and pathway databases

Reactomei REACT_18273. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSi ZBTB17. human.
EvolutionaryTracei Q13105.
GeneWikii ZBTB17.
GenomeRNAii 7709.
NextBioi 29884.
PROi Q13105.
SOURCEi Search...

Gene expression databases

Bgeei Q13105.
CleanExi HS_ZBTB17.
Genevestigatori Q13105.

Family and domain databases

Gene3Di 3.30.160.60. 13 hits.
3.30.710.10. 1 hit.
InterProi 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 ]
Pfami PF00651. BTB. 1 hit.
[Graphical view ]
SMARTi SM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 13 hits.
[Graphical view ]
SUPFAMi SSF54695. SSF54695. 1 hit.
PROSITEi PS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 13 hits.
PS50157. ZINC_FINGER_C2H2_2. 13 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. "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.

Entry informationi

Entry nameiZBT17_HUMAN
AccessioniPrimary (citable) accession number: Q13105
Secondary accession number(s): A0AV07
, B4DXB4, B7ZLQ9, F5H411, Q15932, Q5JYB2, Q9NUC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 26, 2005
Last modified: October 29, 2014
This is version 154 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3