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Protein

Zinc finger and BTB domain-containing protein 37

Gene

ZBTB37

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

May be involved in transcriptional regulation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri373 – 39523C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri401 – 42323C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri429 – 45224C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger and BTB domain-containing protein 37
Gene namesi
Name:ZBTB37
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:28365. ZBTB37.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134911383.

Polymorphism and mutation databases

BioMutaiZBTB37.
DMDMi68566168.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Zinc finger and BTB domain-containing protein 37PRO_0000047741Add
BLAST

Proteomic databases

EPDiQ5TC79.
PaxDbiQ5TC79.
PeptideAtlasiQ5TC79.
PRIDEiQ5TC79.

PTM databases

iPTMnetiQ5TC79.
PhosphoSiteiQ5TC79.

Expressioni

Gene expression databases

BgeeiQ5TC79.
CleanExiHS_ZBTB37.
ExpressionAtlasiQ5TC79. baseline and differential.
GenevisibleiQ5TC79. HS.

Organism-specific databases

HPAiHPA023438.

Interactioni

Protein-protein interaction databases

BioGridi124146. 3 interactions.
IntActiQ5TC79. 3 interactions.
STRINGi9606.ENSP00000356674.

Structurei

3D structure databases

ProteinModelPortaliQ5TC79.
SMRiQ5TC79. Positions 7-144, 378-438.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 9665BTBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri373 – 39523C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri401 – 42323C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri429 – 45224C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000119063.
HOGENOMiHOG000043096.
HOVERGENiHBG055639.
InParanoidiQ5TC79.
KOiK10509.
OMAiKHPERPP.
OrthoDBiEOG7Q8CN4.
PhylomeDBiQ5TC79.
TreeFamiTF331184.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
PF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5TC79-1) [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
MEKGGNIQLE IPDFSNSVLS HLNQLRMQGR LCDIVVNVQG QAFRAHKVVL
60 70 80 90 100
AASSPYFRDH MSLNEMSTVS ISVIKNPTVF EQLLSFCYTG RICLQLADII
110 120 130 140 150
SYLTAASFLQ MQHIIDKCTQ ILEGIHFKIN VAEVEAELSQ TRTKHQERPP
160 170 180 190 200
ESHRVTPNLN RSLSPRHNTP KGNRRGQVSA VLDIRELSPP EESTSPQIIE
210 220 230 240 250
PSSDVESREP ILRINRAGQW YVETGVADRG GRSDDEVRVL GAVHIKTENL
260 270 280 290 300
EEWLGPENQP SGEDGSSAEE VTAMVIDTTG HGSVGQENYT LGSSGAKVAR
310 320 330 340 350
PTSSEVDRFS PSGSVVPLTE RHRARSESPG RMDEPKQPSS QVEESAMMGV
360 370 380 390 400
SGYVEYLREQ EVSERWFRYN PRLTCIYCAK SFNQKGSLDR HMRLHMGITP
410 420 430 440 450
FVCRMCGKKY TRKDQLEYHI RKHTGNKPFH CHVCGKSFPF QAILNQHFRK
460 470 480 490 500
NHPGCIPLEG PHSISPETTV TSRGQAEEES PSQEETVAPG EAVQGSVSTT

GPD
Note: No experimental confirmation available.
Length:503
Mass (Da):56,055
Last modified:December 21, 2004 - v1
Checksum:i169ECA3DBB556A7B
GO
Isoform 2 (identifier: Q5TC79-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     343-361: EESAMMGVSGYVEYLREQE → WSCGFRTALVVGGIATVYE
     362-503: Missing.

Note: No experimental confirmation available.
Show »
Length:361
Mass (Da):39,767
Checksum:i4CAC555491F1AADB
GO
Isoform 3 (identifier: Q5TC79-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     309-503: Missing.

Note: No experimental confirmation available.
Show »
Length:308
Mass (Da):34,036
Checksum:i2FCC9EF3CBF952E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531H → R in BAB71422 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei309 – 503195Missing in isoform 3. 1 PublicationVSP_014440Add
BLAST
Alternative sequencei343 – 36119EESAM…LREQE → WSCGFRTALVVGGIATVYE in isoform 2. 1 PublicationVSP_014441Add
BLAST
Alternative sequencei362 – 503142Missing in isoform 2. 1 PublicationVSP_014442Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK057310 mRNA. Translation: BAB71422.1.
AL136170 Genomic DNA. Translation: CAI19420.1.
AL136170 Genomic DNA. Translation: CAI19421.1.
AL136170 Genomic DNA. Translation: CAI19422.1.
BC003116 mRNA. Translation: AAH03116.1.
BC006315 mRNA. Translation: AAH06315.1.
CCDSiCCDS1312.1. [Q5TC79-2]
CCDS44278.1. [Q5TC79-1]
RefSeqiNP_001116242.1. NM_001122770.1. [Q5TC79-1]
NP_115911.1. NM_032522.3. [Q5TC79-2]
XP_005245603.1. XM_005245546.1. [Q5TC79-1]
XP_006711641.1. XM_006711578.2. [Q5TC79-1]
XP_011508364.1. XM_011510062.1. [Q5TC79-3]
XP_011508365.1. XM_011510063.1. [Q5TC79-3]
UniGeneiHs.668497.

Genome annotation databases

EnsembliENST00000367701; ENSP00000356674; ENSG00000185278. [Q5TC79-1]
ENST00000367702; ENSP00000356675; ENSG00000185278. [Q5TC79-2]
ENST00000367704; ENSP00000356677; ENSG00000185278. [Q5TC79-3]
ENST00000427304; ENSP00000415293; ENSG00000185278. [Q5TC79-1]
GeneIDi84614.
KEGGihsa:84614.
UCSCiuc001gjp.1. human. [Q5TC79-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK057310 mRNA. Translation: BAB71422.1.
AL136170 Genomic DNA. Translation: CAI19420.1.
AL136170 Genomic DNA. Translation: CAI19421.1.
AL136170 Genomic DNA. Translation: CAI19422.1.
BC003116 mRNA. Translation: AAH03116.1.
BC006315 mRNA. Translation: AAH06315.1.
CCDSiCCDS1312.1. [Q5TC79-2]
CCDS44278.1. [Q5TC79-1]
RefSeqiNP_001116242.1. NM_001122770.1. [Q5TC79-1]
NP_115911.1. NM_032522.3. [Q5TC79-2]
XP_005245603.1. XM_005245546.1. [Q5TC79-1]
XP_006711641.1. XM_006711578.2. [Q5TC79-1]
XP_011508364.1. XM_011510062.1. [Q5TC79-3]
XP_011508365.1. XM_011510063.1. [Q5TC79-3]
UniGeneiHs.668497.

3D structure databases

ProteinModelPortaliQ5TC79.
SMRiQ5TC79. Positions 7-144, 378-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124146. 3 interactions.
IntActiQ5TC79. 3 interactions.
STRINGi9606.ENSP00000356674.

PTM databases

iPTMnetiQ5TC79.
PhosphoSiteiQ5TC79.

Polymorphism and mutation databases

BioMutaiZBTB37.
DMDMi68566168.

Proteomic databases

EPDiQ5TC79.
PaxDbiQ5TC79.
PeptideAtlasiQ5TC79.
PRIDEiQ5TC79.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367701; ENSP00000356674; ENSG00000185278. [Q5TC79-1]
ENST00000367702; ENSP00000356675; ENSG00000185278. [Q5TC79-2]
ENST00000367704; ENSP00000356677; ENSG00000185278. [Q5TC79-3]
ENST00000427304; ENSP00000415293; ENSG00000185278. [Q5TC79-1]
GeneIDi84614.
KEGGihsa:84614.
UCSCiuc001gjp.1. human. [Q5TC79-1]

Organism-specific databases

CTDi84614.
GeneCardsiZBTB37.
HGNCiHGNC:28365. ZBTB37.
HPAiHPA023438.
neXtProtiNX_Q5TC79.
PharmGKBiPA134911383.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000119063.
HOGENOMiHOG000043096.
HOVERGENiHBG055639.
InParanoidiQ5TC79.
KOiK10509.
OMAiKHPERPP.
OrthoDBiEOG7Q8CN4.
PhylomeDBiQ5TC79.
TreeFamiTF331184.

Miscellaneous databases

ChiTaRSiZBTB37. human.
GenomeRNAii84614.
PROiQ5TC79.

Gene expression databases

BgeeiQ5TC79.
CleanExiHS_ZBTB37.
ExpressionAtlasiQ5TC79. baseline and differential.
GenevisibleiQ5TC79. HS.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
PF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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.
  2. "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].
  3. "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 2).
    Tissue: Brain.

Entry informationi

Entry nameiZBT37_HUMAN
AccessioniPrimary (citable) accession number: Q5TC79
Secondary accession number(s): Q5TC80, Q96M87, Q9BQ88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 21, 2004
Last modified: July 6, 2016
This is version 113 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.