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ZDBF2_HUMAN
ID   ZDBF2_HUMAN             Reviewed;        2354 AA.
AC   Q9HCK1; Q6ZNP7; Q6ZSN8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 3.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=DBF4-type zinc finger-containing protein 2;
GN   Name=ZDBF2; Synonyms=KIAA1571;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1091 AND 1118-1840.
RC   TISSUE=Hippocampus, and Umbilical cord;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 576-2354.
RC   TISSUE=Brain;
RX   PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA   Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [3]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC85454.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK130893; BAC85454.1; ALT_INIT; mRNA.
DR   EMBL; AK127271; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AB046791; BAB13397.2; -; mRNA.
DR   CCDS; CCDS46501.1; -.
DR   RefSeq; NP_065974.1; NM_020923.2.
DR   RefSeq; XP_005246768.1; XM_005246711.3.
DR   RefSeq; XP_005246769.1; XM_005246712.4.
DR   RefSeq; XP_005246770.1; XM_005246713.3.
DR   RefSeq; XP_006712719.1; XM_006712656.3.
DR   RefSeq; XP_011509834.1; XM_011511532.2.
DR   RefSeq; XP_011509835.1; XM_011511533.2.
DR   RefSeq; XP_011509836.1; XM_011511534.2.
DR   RefSeq; XP_011509837.1; XM_011511535.2.
DR   AlphaFoldDB; Q9HCK1; -.
DR   SMR; Q9HCK1; -.
DR   BioGRID; 121710; 44.
DR   IntAct; Q9HCK1; 17.
DR   MINT; Q9HCK1; -.
DR   STRING; 9606.ENSP00000363545; -.
DR   GlyGen; Q9HCK1; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9HCK1; -.
DR   PhosphoSitePlus; Q9HCK1; -.
DR   BioMuta; ZDBF2; -.
DR   DMDM; 166228734; -.
DR   EPD; Q9HCK1; -.
DR   jPOST; Q9HCK1; -.
DR   MassIVE; Q9HCK1; -.
DR   MaxQB; Q9HCK1; -.
DR   PaxDb; Q9HCK1; -.
DR   PeptideAtlas; Q9HCK1; -.
DR   PRIDE; Q9HCK1; -.
DR   ProteomicsDB; 81743; -.
DR   Antibodypedia; 63267; 14 antibodies from 6 providers.
DR   Ensembl; ENST00000374423.9; ENSP00000363545.3; ENSG00000204186.10.
DR   Ensembl; ENST00000636761.3; ENSP00000490610.1; ENSG00000283649.4.
DR   Ensembl; ENST00000649650.1; ENSP00000497308.1; ENSG00000204186.10.
DR   Ensembl; ENST00000649768.1; ENSP00000498089.1; ENSG00000283649.4.
DR   GeneID; 57683; -.
DR   KEGG; hsa:57683; -.
DR   MANE-Select; ENST00000374423.9; ENSP00000363545.3; NM_020923.3; NP_065974.1.
DR   UCSC; uc002vbp.4; human.
DR   CTD; 57683; -.
DR   DisGeNET; 57683; -.
DR   GeneCards; ZDBF2; -.
DR   HGNC; HGNC:29313; ZDBF2.
DR   HPA; ENSG00000204186; Low tissue specificity.
DR   neXtProt; NX_Q9HCK1; -.
DR   OpenTargets; ENSG00000204186; -.
DR   PharmGKB; PA162409574; -.
DR   VEuPathDB; HostDB:ENSG00000204186; -.
DR   eggNOG; ENOG502RXIX; Eukaryota.
DR   GeneTree; ENSGT00440000037606; -.
DR   HOGENOM; CLU_230228_0_0_1; -.
DR   InParanoid; Q9HCK1; -.
DR   OMA; MGFHADA; -.
DR   OrthoDB; 87289at2759; -.
DR   PhylomeDB; Q9HCK1; -.
DR   TreeFam; TF339806; -.
DR   PathwayCommons; Q9HCK1; -.
DR   SignaLink; Q9HCK1; -.
DR   BioGRID-ORCS; 57683; 7 hits in 1071 CRISPR screens.
DR   ChiTaRS; ZDBF2; human.
DR   GenomeRNAi; 57683; -.
DR   Pharos; Q9HCK1; Tdark.
DR   PRO; PR:Q9HCK1; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9HCK1; protein.
DR   Bgee; ENSG00000204186; Expressed in adrenal tissue and 99 other tissues.
DR   ExpressionAtlas; Q9HCK1; baseline and differential.
DR   Genevisible; Q9HCK1; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043045; P:DNA methylation involved in embryo development; IBA:GO_Central.
DR   GO; GO:0071514; P:genomic imprinting; IBA:GO_Central.
DR   Gene3D; 6.10.250.3410; -; 1.
DR   InterPro; IPR038890; ZDBF2.
DR   InterPro; IPR006572; Znf_DBF.
DR   InterPro; IPR038545; Znf_DBF_sf.
DR   PANTHER; PTHR21639; PTHR21639; 1.
DR   Pfam; PF07535; zf-DBF; 1.
DR   SMART; SM00586; ZnF_DBF; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..2354
FT                   /note="DBF4-type zinc finger-containing protein 2"
FT                   /id="PRO_0000314166"
FT   ZN_FING         1..50
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   REGION          85..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1352..1375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1680..1736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1752..1793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2280..2326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          636..660
FT                   /evidence="ECO:0000255"
FT   COILED          1080..1110
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        85..106
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..886
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1357..1375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1680..1697
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1699..1713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1763..1789
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   BINDING         11
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   MOD_RES         539
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983"
FT   VARIANT         160
FT                   /note="R -> K (in dbSNP:rs10932150)"
FT                   /id="VAR_037853"
SQ   SEQUENCE   2354 AA;  265618 MW;  4B72E43A76CED774 CRC64;
     MQKRQGYCSY CRVQYNNLEQ HLFSAQHRSL TRQSRRQICT SSLMERFLQD VLQHHPYHCQ
     ESSSTQDETH VNTGSSSEVV HLDDAFSEEE EEDEDKVEDE DATEERPSEV SEPIEELHSR
     PHKSQEGTQE VSVRPSVIQK LEKGQQQPLE FVHKIGASVR KCNLVDIGQA TNNRSNLVRP
     PVICNAPASC LPESSNDRPV TANTTSLPPA AHLDSVSKCD PNKVEKYLEQ PDGASRNPVP
     SSHVETTSFS YQKHKESNRK SLRMNSDKLV LWKDVKSQGK TLSAGLKFHE RMGTKGSLRV
     KSPSKLAVNP NKTDMPSNKG IFEDTIAKNH EEFFSNMDCT QEEKHLVFNK TAFWEQKCSV
     SSEMKFDCIS LQSASDQPQE TAQDLSLWKE EQIDQEDNYE SRGSEMSFDC SSSFHSLTDQ
     SKVSAKEVNL SKEVRTDVQY KNNKSYVSKI SSDCDDILHL VTNQSQMIVK EISLQNARHI
     SLVDQSYESS SSETNFDCDA SPQSTSDYPQ QSVTEVNLPK EVHIGLVDKN YGSSSSEVSA
     DSVFPLQSVV DRPPVAVTET KLRKKAHTSL VDNYGSSCSE TSFDCDVSLE SVVDHPQLTV
     KGRNLKGRQV HLKHKKRKPS SAKAHLDCDV SLGTVADESQ RAVEKINLLK EKNADLMDMN
     CESHGPEMGF QADAQLADQS QVAEIERQKV DVDLENKSVQ SSRSSLSSDS PASLYHSAHD
     EPQEALDEVN LKELNIDMEV RSYDCSSSEL TFDSDPPLLS VTEQSHLDAE GKERHIDLED
     ESCESDSSEI TFDSDIPLYS VIDQPEVAVY EEETVDLESK SNESCVSEIT FDSDIPLHSG
     NDHPEVAVKE VIQKEEYIHL ERKNDEPSGS EISSDSHAPL HSVTNSPEVA VKKLNPQKEE
     QVHLENKENE PIDSEVSLDY NIIFHSVTGR SEDPIKEISL HTKEHMYLEN KSVFETSLDS
     DVPLQAATHK PEVIVKETWL QREKHAEFQG RSTEFSGSKT SLDSGVPHYS VTEPQVAVNK
     INRKKQYVLE NKNDKCSGSE IILDSNVPPQ SMTDQPQLAF LKEKHVNLKD KNSKSGDSKI
     TFDSEQLQEA VKKIDQWKEE VIGLKNKINE PSTYKLIHHP DVSVQSVADQ PKVAIKHVNL
     GNENHMYLEV KNSQYSCSEM NLDSGFLGQS IVNRPQITIL EQEHIELEGK HNQCCGSEVS
     FDSDDPLQSV ADRLRETVKE ISLWKDEEVD TEDRRNEAKG FEIMYDSDVL QPVAGQPEEV
     VKEVSLWKEH VDLENKIVKP TDSRINFDSH EPLQSVTNKI PGANKEINLL REEHVCLDDK
     GYVPSDSEII YVSNIPLQSV IKQPHILEEE HASLEDKSSN SYSPEESSDS NDSFQAAADE
     LQKPVKEINL WKEDHIYLED KSYKLGDFDV SYASHIPVQF VTDQSSVPVK EINLQKKDHN
     DLENKNCEVC GSEIKCHSCV HLQSEVDQPQ VSYKEADLQK EEHVVMEEKT DQPSDSEMMY
     DSDVPFQIVV NQFPGSVKET HLPKVVLVDL VPGDSDYEVI SDDIPLQLVT DPPQLTVKDI
     SCINTECIDI EDKSCDFFGS EVRCNCKAST PSMTNQCKET FKIINRKKDY IILGEPSCQS
     CGSEMNFNVD ASDQSMTYES QGPDEKMVKY IDSEDKSCGY NGSKGKFNLE DTSHRTTHRL
     QKAHKEASLR KDPRNAGLKG KSCQSSASAV DFGASSKSAL HRRADKKKRS KLKHRDLEVS
     CEPDGFEMNF QCAPPLPSDT DQPQETVKKR HPCKKVSSDL KEKNHDSQSS SVLKVDSVRN
     LKKAKDVIED NPDEPVLEAL PHVPPSFVGK TWSQIMREDD IKINALVKEF REGRFHCYFD
     DDCETKKVSS KGKKKVTWAD LQGKEDTAPT QAVSESDDIV CGISDIDDLS VALDKPCHRH
     PPAERPPKQK GRVASQCQTA KISHSTQTSC KNYPVMKRKI IRQEEDPPKS KCSRLQDDRK
     TKKKVKIGTV EFPASCTKVL KPMQPKALVC VLSSLNIKLK EGEGLPFPKM RHHSWDNDIR
     FICKYKRNIF DYYEPLIKQI VISPPLSVIV PEFERRNWVK IHFNRSNQNS SAGDNDADGQ
     GSASAPLMAV PARYGFNSHQ GTSDSSLFLE ESKVLHAREL PKKRNFQLTF LNHDVVKISP
     KSVRNKLLES QSKKKIHGKR VTTSSNKLGF PKKVYKPIIL QQKPRKASEK QSIWIRTKPS
     DIIRKYISKY SVFLRHRYQS RSAFLGRYLK KKKSVVSRLK KAKRTAKVLL NSSVPPAGAE
     ELSSAMANPP PKRPVRASCR VARRRKKTDE SYHGRQKGPS TPVRAYDLRS SSCLQQRERM
     MTRLANKLRG NEVK
 
 
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