ZN639_HUMAN
ID ZN639_HUMAN Reviewed; 485 AA.
AC Q9UID6; A9X3Z9; D3DNR3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Zinc finger protein 639;
DE AltName: Full=Zinc finger protein ANC_2H01;
DE AltName: Full=Zinc finger protein ZASC1;
GN Name=ZNF639; Synonyms=ZASC1;
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 [MRNA], FUNCTION, INTERACTION WITH CTNNA2, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=16182284; DOI=10.1016/j.yexcr.2005.06.018;
RA Bogaerts S., Vanlandschoot A., van Hengel J., van Roy F.;
RT "Nuclear translocation of alphaN-catenin by the novel zinc finger
RT transcriptional repressor ZASC1.";
RL Exp. Cell Res. 311:1-13(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=14522885;
RA Imoto I., Yuki Y., Sonoda I., Ito T., Shimada Y., Imamura M., Inazawa J.;
RT "Identification of ZASC1 encoding a Kruppel-like zinc finger protein as a
RT novel target for 3q26 amplification in esophageal squamous cell
RT carcinomas.";
RL Cancer Res. 63:5691-5696(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Uterus;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-190.
RX PubMed=17623809; DOI=10.1101/gr.6320607;
RA Krull M., Petrusma M., Makalowski W., Brosius J., Schmitz J.;
RT "Functional persistence of exonized mammalian-wide interspersed repeat
RT elements (MIRs).";
RL Genome Res. 17:1139-1145(2007).
RN [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-88, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-177; LYS-181 AND LYS-226,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Binds DNA and may function as a transcriptional repressor.
CC {ECO:0000269|PubMed:16182284}.
CC -!- SUBUNIT: Interacts with CTNNA2. {ECO:0000269|PubMed:16182284}.
CC -!- INTERACTION:
CC Q9UID6; P26232: CTNNA2; NbExp=7; IntAct=EBI-947476, EBI-3953920;
CC Q9UID6; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-947476, EBI-21603100;
CC Q9UID6; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-947476, EBI-348259;
CC Q9UID6; Q00013: MPP1; NbExp=3; IntAct=EBI-947476, EBI-711788;
CC Q9UID6; Q96T60: PNKP; NbExp=6; IntAct=EBI-947476, EBI-1045072;
CC Q9UID6; Q99633: PRPF18; NbExp=5; IntAct=EBI-947476, EBI-2798416;
CC Q9UID6; Q8N680: ZBTB2; NbExp=5; IntAct=EBI-947476, EBI-2515601;
CC Q9UID6; O43167: ZBTB24; NbExp=3; IntAct=EBI-947476, EBI-744471;
CC Q9UID6; P15622-3: ZNF250; NbExp=3; IntAct=EBI-947476, EBI-10177272;
CC Q9UID6; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-947476, EBI-10240849;
CC Q9UID6; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-947476, EBI-11962574;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14522885,
CC ECO:0000269|PubMed:16182284}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF003924; AAF21240.1; -; mRNA.
DR EMBL; AB097862; BAC77610.1; -; mRNA.
DR EMBL; AC007823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78413.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78414.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78415.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78416.1; -; Genomic_DNA.
DR EMBL; BC020500; AAH20500.1; -; mRNA.
DR EMBL; BC026181; AAH26181.1; -; mRNA.
DR EMBL; DQ323613; ABD27860.1; -; mRNA.
DR CCDS; CCDS3227.1; -.
DR RefSeq; NP_001290354.1; NM_001303425.1.
DR RefSeq; NP_001290355.1; NM_001303426.1.
DR RefSeq; NP_057415.1; NM_016331.2.
DR RefSeq; XP_016862039.1; XM_017006550.1.
DR RefSeq; XP_016862040.1; XM_017006551.1.
DR RefSeq; XP_016862041.1; XM_017006552.1.
DR RefSeq; XP_016862042.1; XM_017006553.1.
DR AlphaFoldDB; Q9UID6; -.
DR SMR; Q9UID6; -.
DR BioGRID; 119367; 41.
DR IntAct; Q9UID6; 22.
DR STRING; 9606.ENSP00000325634; -.
DR iPTMnet; Q9UID6; -.
DR PhosphoSitePlus; Q9UID6; -.
DR BioMuta; ZNF639; -.
DR DMDM; 51316968; -.
DR EPD; Q9UID6; -.
DR jPOST; Q9UID6; -.
DR MassIVE; Q9UID6; -.
DR MaxQB; Q9UID6; -.
DR PaxDb; Q9UID6; -.
DR PeptideAtlas; Q9UID6; -.
DR PRIDE; Q9UID6; -.
DR ProteomicsDB; 84496; -.
DR ABCD; Q9UID6; 2 sequenced antibodies.
DR Antibodypedia; 46810; 79 antibodies from 19 providers.
DR DNASU; 51193; -.
DR Ensembl; ENST00000326361.7; ENSP00000325634.3; ENSG00000121864.10.
DR Ensembl; ENST00000484866.5; ENSP00000418766.1; ENSG00000121864.10.
DR Ensembl; ENST00000496856.6; ENSP00000417740.1; ENSG00000121864.10.
DR Ensembl; ENST00000621687.1; ENSP00000477626.1; ENSG00000121864.10.
DR GeneID; 51193; -.
DR KEGG; hsa:51193; -.
DR MANE-Select; ENST00000496856.6; ENSP00000417740.1; NM_001303426.2; NP_001290355.1.
DR UCSC; uc003fjq.2; human.
DR CTD; 51193; -.
DR DisGeNET; 51193; -.
DR GeneCards; ZNF639; -.
DR HGNC; HGNC:30950; ZNF639.
DR HPA; ENSG00000121864; Low tissue specificity.
DR MIM; 619214; gene.
DR neXtProt; NX_Q9UID6; -.
DR OpenTargets; ENSG00000121864; -.
DR PharmGKB; PA134990796; -.
DR VEuPathDB; HostDB:ENSG00000121864; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156335; -.
DR HOGENOM; CLU_569800_0_0_1; -.
DR InParanoid; Q9UID6; -.
DR OMA; HLQIHET; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9UID6; -.
DR TreeFam; TF335557; -.
DR PathwayCommons; Q9UID6; -.
DR SignaLink; Q9UID6; -.
DR BioGRID-ORCS; 51193; 13 hits in 1097 CRISPR screens.
DR GenomeRNAi; 51193; -.
DR Pharos; Q9UID6; Tbio.
DR PRO; PR:Q9UID6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UID6; protein.
DR Bgee; ENSG00000121864; Expressed in cortical plate and 181 other tissues.
DR ExpressionAtlas; Q9UID6; baseline and differential.
DR Genevisible; Q9UID6; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0046718; P:viral entry into host cell; IDA:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..485
FT /note="Zinc finger protein 639"
FT /id="PRO_0000047696"
FT ZN_FING 204..227
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 233..255
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 260..283
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..311
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..397
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..425
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..454
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 460..482
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..455
FT /note="Interaction with CTNNA2"
FT /evidence="ECO:0000269|PubMed:16182284"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 485 AA; 56054 MW; BDEB00B87BCC1C1C CRC64;
MNEYPKKRKR KTLHPSRYSD SSGISRIADG FNGIFSDHCY SVCSMRQPDL KYFDNKDDDS
DTETSNDLPK FADGIKARNR NQNYLVPSPV LRILDHTAFS TEKSADIVIC DEECDSPESV
NQQTQEESPI EVHTAEDVPI AVEVHAISED YDIETENNSS ESLQDQTDEE PPAKLCKILD
KSQALNVTAQ QKWPLLRANS SGLYKCELCE FNSKYFSDLK QHMILKHKRT DSNVCRVCKE
SFSTNMLLIE HAKLHEEDPY ICKYCDYKTV IFENLSQHIA DTHFSDHLYW CEQCDVQFSS
SSELYLHFQE HSCDEQYLCQ FCEHETNDPE DLHSHVVNEH ACKLIELSDK YNNGEHGQYS
LLSKITFDKC KNFFVCQVCG FRSRLHTNVN RHVAIEHTKI FPHVCDDCGK GFSSMLEYCK
HLNSHLSEGI YLCQYCEYST GQIEDLKIHL DFKHSADLPH KCSDCLMRFG NERELISHLP
VHETT
