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ZN433_HUMAN
ID   ZN433_HUMAN             Reviewed;         673 AA.
AC   Q8N7K0; Q86VX3;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Zinc finger protein 433;
GN   Name=ZNF433;
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] (ISOFORM 1).
RC   TISSUE=Uterus;
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 GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- INTERACTION:
CC       Q8N7K0; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-10267553, EBI-739624;
CC       Q8N7K0; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-10267553, EBI-10172150;
CC       Q8N7K0; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10267553, EBI-10172290;
CC       Q8N7K0; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-10267553, EBI-10172052;
CC       Q8N7K0; Q99750: MDFI; NbExp=3; IntAct=EBI-10267553, EBI-724076;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8N7K0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N7K0-2; Sequence=VSP_035523;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AK098300; BAC05279.1; -; mRNA.
DR   EMBL; CH471106; EAW84254.1; -; Genomic_DNA.
DR   EMBL; BC047412; AAH47412.1; -; mRNA.
DR   CCDS; CCDS45983.1; -. [Q8N7K0-1]
DR   CCDS; CCDS77240.1; -. [Q8N7K0-2]
DR   RefSeq; NP_001073880.1; NM_001080411.2. [Q8N7K0-1]
DR   RefSeq; NP_001295275.1; NM_001308346.1.
DR   RefSeq; NP_001295277.1; NM_001308348.1.
DR   RefSeq; NP_001295280.1; NM_001308351.1. [Q8N7K0-2]
DR   RefSeq; NP_001295284.1; NM_001308355.1. [Q8N7K0-2]
DR   RefSeq; NP_001295286.1; NM_001308357.1. [Q8N7K0-2]
DR   RefSeq; XP_006722724.1; XM_006722661.3. [Q8N7K0-2]
DR   AlphaFoldDB; Q8N7K0; -.
DR   SMR; Q8N7K0; -.
DR   BioGRID; 127846; 9.
DR   IntAct; Q8N7K0; 7.
DR   STRING; 9606.ENSP00000339767; -.
DR   GlyGen; Q8N7K0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8N7K0; -.
DR   PhosphoSitePlus; Q8N7K0; -.
DR   BioMuta; ZNF433; -.
DR   DMDM; 30173446; -.
DR   jPOST; Q8N7K0; -.
DR   MassIVE; Q8N7K0; -.
DR   MaxQB; Q8N7K0; -.
DR   PaxDb; Q8N7K0; -.
DR   PeptideAtlas; Q8N7K0; -.
DR   PRIDE; Q8N7K0; -.
DR   Antibodypedia; 25988; 138 antibodies from 20 providers.
DR   DNASU; 163059; -.
DR   Ensembl; ENST00000344980.11; ENSP00000339767.6; ENSG00000197647.13. [Q8N7K0-1]
DR   Ensembl; ENST00000419886.7; ENSP00000393416.2; ENSG00000197647.13. [Q8N7K0-2]
DR   Ensembl; ENST00000547560.6; ENSP00000448806.2; ENSG00000197647.13. [Q8N7K0-2]
DR   Ensembl; ENST00000552904.6; ENSP00000448233.2; ENSG00000197647.13. [Q8N7K0-2]
DR   GeneID; 163059; -.
DR   KEGG; hsa:163059; -.
DR   UCSC; uc002msy.2; human. [Q8N7K0-1]
DR   CTD; 163059; -.
DR   DisGeNET; 163059; -.
DR   GeneCards; ZNF433; -.
DR   HGNC; HGNC:20811; ZNF433.
DR   HPA; ENSG00000197647; Tissue enhanced (testis).
DR   neXtProt; NX_Q8N7K0; -.
DR   OpenTargets; ENSG00000197647; -.
DR   PharmGKB; PA134943717; -.
DR   VEuPathDB; HostDB:ENSG00000197647; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00950000182755; -.
DR   HOGENOM; CLU_002678_17_1_1; -.
DR   InParanoid; Q8N7K0; -.
DR   OMA; WRRMPSC; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q8N7K0; -.
DR   TreeFam; TF343410; -.
DR   PathwayCommons; Q8N7K0; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q8N7K0; -.
DR   BioGRID-ORCS; 163059; 12 hits in 1070 CRISPR screens.
DR   ChiTaRS; ZNF433; human.
DR   GenomeRNAi; 163059; -.
DR   Pharos; Q8N7K0; Tdark.
DR   PRO; PR:Q8N7K0; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q8N7K0; protein.
DR   Bgee; ENSG00000197647; Expressed in right testis and 102 other tissues.
DR   ExpressionAtlas; Q8N7K0; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 11.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 19.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 10.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..673
FT                   /note="Zinc finger protein 433"
FT                   /id="PRO_0000047581"
FT   DOMAIN          7..85
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         142..164
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         170..192
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         198..220
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         226..248
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         254..276
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         282..304
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         310..332
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         338..360
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         366..388
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         394..416
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         422..444
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         450..472
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         478..500
FT                   /note="C2H2-type 13; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         506..528
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         534..556
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         562..584
FT                   /note="C2H2-type 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         590..612
FT                   /note="C2H2-type 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         618..640
FT                   /note="C2H2-type 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         646..668
FT                   /note="C2H2-type 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   VAR_SEQ         1..35
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035523"
SQ   SEQUENCE   673 AA;  77243 MW;  8C8B1B6D272D08FC CRC64;
     MMFQDSVAFE DVAVTFTQEE WALLDPSQKN LCRDVMQETF RNLASIGKKW KPQNIYVEYE
     NLRRNLRIVG ERLFESKEGH QHGEILTQVP DDMLKKTTTG VKSCESSVYG EVGSAHSSLN
     RHIRDDTGHK AYEYQEYGQK PYKCKYCKKP FNCLSSVQTH ERAHSGRKLY VCEECGKTFI
     SHSNLQRHRI MHRGDGPYKC KFCGKALMFL SLYLIHKRTH TGEKPYQCKQ CGKAFSHSSS
     LRIHERTHTG EKPYKCNECG KAFHSSTCLH AHKRTHTGEK PYECKQCGKA FSSSHSFQIH
     ERTHTGEKPY ECKECGKAFK CPSSVRRHER THSRKKPYEC KHCGKVLSYL TSFQNHLGMH
     TGEISHKCKI CGKAFYSPSS LQTHEKTHTG EKPYKCNQCG KAFNSSSSFR YHERTHTGEK
     PYECKQCGKA FRSASLLQTH GRTHTGEKPY ACKECGKPFS NFSFFQIHER MHREEKPYEC
     KGYGKTFSLP SLFHRHERTH TGGKTYECKQ CGRSFNCSSS FRYHGRTHTG EKPYECKQCG
     KAFRSASQLQ IHGRTHTGEK PYECKQCGKA FGSASHLQMH GRTHTGEKPY ECKQCGKSFG
     CASRLQMHGR THTGEKPYKC KQCGKAFGCP SNLRRHGRTH TGEKPYKCNQ CGKVFRCSSQ
     LQVHGRAHCI DTP
 
 
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