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Protein

Zinc finger and BTB domain-containing protein 38

Gene

ZBTB38

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

Functioni

Transcriptional regulator with bimodal DNA-binding specificity. Binds with a higher affinity to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to E-box elements (5'-CACGTG-3'). Can also bind specifically to a single methyl-CpG pair. Represses transcription in a methyl-CpG-dependent manner (PubMed:16354688). Plays an important role in regulating DNA replication and common fragile sites (CFS) stability in a RBBP6- and MCM10-dependent manner; represses expression of MCM10 which plays an important role in DNA-replication (PubMed:24726359). Acts as a transcriptional activator. May be involved in the differentiation and/or survival of late postmitotic neurons (By similarity).By similarity2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri342 – 36423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri371 – 39525C2H2-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri460 – 48223C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri488 – 51023C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri516 – 53924C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1010 – 103223C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1038 – 106023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1066 – 108823C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1094 – 111623C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1125 – 114723C2H2-type 10PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • methyl-CpG binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of DNA replication Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

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 38
Gene namesi
Name:ZBTB38Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:26636. ZBTB38.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • chromosome Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

MIMi612221. phenotype.
PharmGKBiPA142670542.

Polymorphism and mutation databases

BioMutaiZBTB38.
DMDMi68566212.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11951195Zinc finger and BTB domain-containing protein 38PRO_0000047742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki43 – 43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei130 – 1301PhosphoserineCombined sources
Cross-linki145 – 145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei309 – 3091PhosphoserineCombined sources
Cross-linki557 – 557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki758 – 758Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki814 – 814Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki977 – 977Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Ubiquitinated by RBBP6; leading to its degradation by the proteasome.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8NAP3.
MaxQBiQ8NAP3.
PaxDbiQ8NAP3.
PeptideAtlasiQ8NAP3.
PRIDEiQ8NAP3.

PTM databases

iPTMnetiQ8NAP3.
PhosphoSiteiQ8NAP3.

Expressioni

Gene expression databases

BgeeiQ8NAP3.
CleanExiHS_ZBTB38.
ExpressionAtlasiQ8NAP3. baseline and differential.
GenevisibleiQ8NAP3. HS.

Organism-specific databases

HPAiHPA014865.

Interactioni

Subunit structurei

Interacts with CBFA2T3. Interacts with ZBTB4. Interacts with RBBP6.3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi128969. 47 interactions.
IntActiQ8NAP3. 4 interactions.
STRINGi9606.ENSP00000406955.

Structurei

3D structure databases

ProteinModelPortaliQ8NAP3.
SMRiQ8NAP3. Positions 448-542.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 10068BTBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni300 – 523224Interaction with CBFA2T31 PublicationAdd
BLAST

Domaini

The BTB domain is not required for activation of transcription or self-association.By similarity

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 10 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri342 – 36423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri371 – 39525C2H2-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri460 – 48223C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri488 – 51023C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri516 – 53924C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1010 – 103223C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1038 – 106023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1066 – 108823C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1094 – 111623C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1125 – 114723C2H2-type 10PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00810000125416.
HOVERGENiHBG084299.
InParanoidiQ8NAP3.
KOiK10510.
OMAiCELCAKQ.
PhylomeDBiQ8NAP3.
TreeFamiTF333100.

Family and domain databases

Gene3Di3.30.160.60. 6 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.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 10 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 9 hits.
PS50157. ZINC_FINGER_C2H2_2. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NAP3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVMSLSRDL KDDFHSDTVL SILNEQRIRG ILCDVTIIVE DTKFKAHSNV
60 70 80 90 100
LAASSLYFKN IFWSHTICIS SHVLELDDLK AEVFTEILNY IYSSTVVVKR
110 120 130 140 150
QETVTDLAAA GKKLGISFLE DLTDRNFSNS PGPYVFCITE KGVVKEEKNE
160 170 180 190 200
KRHEEPAITN GPRITNAFSI IETENSNNMF SPLDLRASFK KVSDSMRTAS
210 220 230 240 250
LCLERTDVCH EAEPVRTLAE HSYAVSSVAE AYRSQPVREH DGSSPGNTGK
260 270 280 290 300
ENCEALAAKP KTCRKPKTFS IPQDSDSATE NIPPPPVSNL EVNQERSPQP
310 320 330 340 350
AAVLTRSKSP NNEGDVHFSR EDENQSSDVP GPPAAEVPPL VYNCSCCSKA
360 370 380 390 400
FDSSTLLSAH MQLHKPTQEP LVCKYCNKQF TTLNRLDRHE QICMRSSHMP
410 420 430 440 450
IPGGNQRFLE NYPTIGQNGG SFTGPEPLLS ENRIGEFSST GSTLPDTDHM
460 470 480 490 500
VKFVNGQMLY SCVVCKRSYV TLSSLRRHAN VHSWRRTYPC HYCNKVFALA
510 520 530 540 550
EYRTRHEIWH TGERRYQCIF CLETFMTYYI LKNHQKSFHA IDHRLSISKK
560 570 580 590 600
TANGGLKPSV YPYKLYRLLP MKCKRAPYKS YRNSSYENAR ENSQMNESAP
610 620 630 640 650
GTYVVQNPHS SELPTLNFQD TVNTLTNSPA IPLETSACQD IPTSANVQNA
660 670 680 690 700
EGTKWGEEAL KMDLDNNFYS TEVSVSSTEN AVSSDLRAGD VPVLSLSNSS
710 720 730 740 750
ENAASVISYS GSAPSVIVHS SQFSSVIMHS NAIAAMTSSN HRAFSDPAVS
760 770 780 790 800
QSLKDDSKPE PDKVGRFASR PKSIKEKKKT TSHTRGEIPE ESNYVADPGG
810 820 830 840 850
SLSKTTNIAE ETSKIETYIA KPALPGTSTN SNVAPLCQIT VKIGNEAIVK
860 870 880 890 900
RHILGSKLFY KRGRRPKYQM QEEPLPQGND PEPSGDSPLG LCQSECMEMS
910 920 930 940 950
EVFDDASDQD STDKPWRPYY NYKPKKKSRQ LKKMRKVNWR KEHGNRSPSH
960 970 980 990 1000
KCKYPAELDC AVGKAPQDKP FEEEETKEMP KLQCELCDGD KAVGAGNQGR
1010 1020 1030 1040 1050
PHRHLTSRPY ACELCAKQFQ SPSTLKMHMR CHTGEKPYQC KTCGRCFSVQ
1060 1070 1080 1090 1100
GNLQKHERIH LGLKEFVCQY CNKAFTLNET LKIHERIHTG EKRYHCQFCF
1110 1120 1130 1140 1150
QRFLYLSTKR NHEQRHIREH NGKGYACFQC PKICKTAAAL GMHQKKHLFK
1160 1170 1180 1190
SPSQQEKIGD VCHENSNPLE NQHFIGSEDN DQKDNIQTGV ENVVL
Length:1,195
Mass (Da):134,257
Last modified:July 5, 2005 - v2
Checksum:iA44561D86ACCC2D8
GO

Sequence cautioni

The sequence BAC03868.1 differs from that shown. Reason: Frameshift at position 147. Curated

Polymorphismi

Genetic variations in ZBTB38 define the stature quantitative trait locus 10 (STQTL10) [MIMi:612221]. Adult height is an easily observable and highly heritable complex continuous trait. Because of this, it is a model trait for studying genetic influence on quantitative traits.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti319 – 3191S → A.
Corresponds to variant rs16851435 [ dbSNP | Ensembl ].
VAR_052917
Natural varianti615 – 6151T → M.
Corresponds to variant rs17787670 [ dbSNP | Ensembl ].
VAR_052918
Natural varianti809 – 8091A → T.
Corresponds to variant rs3732867 [ dbSNP | Ensembl ].
VAR_052919

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010184 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79004.1.
CH471052 Genomic DNA. Translation: EAW79005.1.
AK092355 mRNA. Translation: BAC03868.1. Frameshift.
CCDSiCCDS43157.1.
RefSeqiNP_001073881.2. NM_001080412.2.
XP_005247313.1. XM_005247256.3.
XP_005247314.1. XM_005247257.1.
XP_005247315.1. XM_005247258.1.
XP_005247318.1. XM_005247261.2.
XP_006713622.1. XM_006713559.2.
XP_011510913.1. XM_011512611.1.
UniGeneiHs.518301.

Genome annotation databases

EnsembliENST00000321464; ENSP00000372635; ENSG00000177311.
ENST00000441582; ENSP00000406955; ENSG00000177311.
ENST00000514251; ENSP00000426387; ENSG00000177311.
GeneIDi253461.
KEGGihsa:253461.
UCSCiuc062olr.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC010184 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79004.1.
CH471052 Genomic DNA. Translation: EAW79005.1.
AK092355 mRNA. Translation: BAC03868.1. Frameshift.
CCDSiCCDS43157.1.
RefSeqiNP_001073881.2. NM_001080412.2.
XP_005247313.1. XM_005247256.3.
XP_005247314.1. XM_005247257.1.
XP_005247315.1. XM_005247258.1.
XP_005247318.1. XM_005247261.2.
XP_006713622.1. XM_006713559.2.
XP_011510913.1. XM_011512611.1.
UniGeneiHs.518301.

3D structure databases

ProteinModelPortaliQ8NAP3.
SMRiQ8NAP3. Positions 448-542.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128969. 47 interactions.
IntActiQ8NAP3. 4 interactions.
STRINGi9606.ENSP00000406955.

PTM databases

iPTMnetiQ8NAP3.
PhosphoSiteiQ8NAP3.

Polymorphism and mutation databases

BioMutaiZBTB38.
DMDMi68566212.

Proteomic databases

EPDiQ8NAP3.
MaxQBiQ8NAP3.
PaxDbiQ8NAP3.
PeptideAtlasiQ8NAP3.
PRIDEiQ8NAP3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321464; ENSP00000372635; ENSG00000177311.
ENST00000441582; ENSP00000406955; ENSG00000177311.
ENST00000514251; ENSP00000426387; ENSG00000177311.
GeneIDi253461.
KEGGihsa:253461.
UCSCiuc062olr.1. human.

Organism-specific databases

CTDi253461.
GeneCardsiZBTB38.
H-InvDBHIX0003727.
HGNCiHGNC:26636. ZBTB38.
HPAiHPA014865.
MIMi612218. gene.
612221. phenotype.
neXtProtiNX_Q8NAP3.
PharmGKBiPA142670542.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00810000125416.
HOVERGENiHBG084299.
InParanoidiQ8NAP3.
KOiK10510.
OMAiCELCAKQ.
PhylomeDBiQ8NAP3.
TreeFamiTF333100.

Miscellaneous databases

ChiTaRSiZBTB38. human.
GenomeRNAii253461.
NextBioi92101.
PROiQ8NAP3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NAP3.
CleanExiHS_ZBTB38.
ExpressionAtlasiQ8NAP3. baseline and differential.
GenevisibleiQ8NAP3. HS.

Family and domain databases

Gene3Di3.30.160.60. 6 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.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 10 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 9 hits.
PS50157. ZINC_FINGER_C2H2_2. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] OF 1-775.
    Tissue: BrainImported.
  4. "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-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "A family of human zinc finger proteins that bind methylated DNA and repress transcription."
    Filion G.J., Zhenilo S., Salozhin S., Yamada D., Prokhortchouk E., Defossez P.A.
    Mol. Cell. Biol. 26:169-181(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH ZBTB4.
  6. Cited for: POLYMORPHISM.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: INTERACTION WITH CBFA2T3.
  9. "The RBBP6/ZBTB38/MCM10 axis regulates DNA replication and common fragile site stability."
    Miotto B., Chibi M., Xie P., Koundrioukoff S., Moolman-Smook H., Pugh D., Debatisse M., He F., Zhang L., Defossez P.A.
    Cell Rep. 7:575-587(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RBBP6, UBIQUITINATION.
  10. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43; LYS-145; LYS-758; LYS-814 AND LYS-977, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43; LYS-145 AND LYS-758, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43; LYS-145; LYS-557 AND LYS-977, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZBT38_HUMAN
AccessioniPrimary (citable) accession number: Q8NAP3
Secondary accession number(s): D3DNF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: April 13, 2016
This is version 121 of the entry and version 2 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.