ID   ZN136_HUMAN             Reviewed;         540 AA.
AC   P52737;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 192.
DE   RecName: Full=Zinc finger protein 136;
GN   Name=ZNF136;
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].
RC   TISSUE=Insulinoma;
RX   PubMed=7649249; DOI=10.1016/0014-5793(95)00728-r;
RA   Vissing H., Meyer W.-K., Aagaard L., Tommerup N., Thiesen H.-J.;
RT   "Repression of transcriptional activity by heterologous KRAB domains
RT   present in zinc finger proteins.";
RL   FEBS Lett. 369:153-157(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Insulinoma;
RX   PubMed=7557990; DOI=10.1006/geno.1995.1040;
RA   Tommerup N., Vissing H.;
RT   "Isolation and fine mapping of 16 novel human zinc finger-encoding cDNAs
RT   identify putative candidate genes for developmental and malignant
RT   disorders.";
RL   Genomics 27:259-264(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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).
CC   -!- FUNCTION: May be involved in transcriptional regulation as a weak
CC       repressor when alone, or a potent one when fused with a heterologous
CC       protein containing a KRAB B-domain.
CC   -!- INTERACTION:
CC       P52737; O95273: CCNDBP1; NbExp=5; IntAct=EBI-749129, EBI-748961;
CC       P52737; Q8NHQ1: CEP70; NbExp=5; IntAct=EBI-749129, EBI-739624;
CC       P52737; P49760: CLK2; NbExp=3; IntAct=EBI-749129, EBI-750020;
CC       P52737; Q99750: MDFI; NbExp=12; IntAct=EBI-749129, EBI-724076;
CC       P52737; Q5JR59: MTUS2; NbExp=4; IntAct=EBI-749129, EBI-742948;
CC       P52737; Q5JR59-3: MTUS2; NbExp=4; IntAct=EBI-749129, EBI-11522433;
CC       P52737; Q16623: STX1A; NbExp=3; IntAct=EBI-749129, EBI-712466;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Seems ubiquitous. Seen in the heart, brain,
CC       placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; U09367; AAC50261.1; -; mRNA.
DR   EMBL; BC006421; AAH06421.1; -; mRNA.
DR   CCDS; CCDS32916.1; -.
DR   PIR; B57785; B57785.
DR   RefSeq; NP_001334942.1; NM_001348013.1.
DR   RefSeq; NP_001334943.1; NM_001348014.1.
DR   RefSeq; NP_003428.1; NM_003437.4.
DR   AlphaFoldDB; P52737; -.
DR   SMR; P52737; -.
DR   BioGRID; 113490; 48.
DR   IntAct; P52737; 9.
DR   MINT; P52737; -.
DR   STRING; 9606.ENSP00000344162; -.
DR   iPTMnet; P52737; -.
DR   PhosphoSitePlus; P52737; -.
DR   BioMuta; ZNF136; -.
DR   DMDM; 1731412; -.
DR   EPD; P52737; -.
DR   jPOST; P52737; -.
DR   MassIVE; P52737; -.
DR   MaxQB; P52737; -.
DR   PaxDb; P52737; -.
DR   PeptideAtlas; P52737; -.
DR   PRIDE; P52737; -.
DR   ProteomicsDB; 56510; -.
DR   Antibodypedia; 13233; 133 antibodies from 21 providers.
DR   DNASU; 7695; -.
DR   Ensembl; ENST00000343979.6; ENSP00000344162.4; ENSG00000196646.12.
DR   GeneID; 7695; -.
DR   KEGG; hsa:7695; -.
DR   MANE-Select; ENST00000343979.6; ENSP00000344162.4; NM_003437.5; NP_003428.1.
DR   UCSC; uc002mti.4; human.
DR   CTD; 7695; -.
DR   DisGeNET; 7695; -.
DR   GeneCards; ZNF136; -.
DR   HGNC; HGNC:12920; ZNF136.
DR   HPA; ENSG00000196646; Low tissue specificity.
DR   MIM; 604078; gene.
DR   neXtProt; NX_P52737; -.
DR   OpenTargets; ENSG00000196646; -.
DR   PharmGKB; PA37508; -.
DR   VEuPathDB; HostDB:ENSG00000196646; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000164354; -.
DR   HOGENOM; CLU_002678_44_3_1; -.
DR   InParanoid; P52737; -.
DR   OMA; HYKHQGR; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P52737; -.
DR   TreeFam; TF338854; -.
DR   PathwayCommons; P52737; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; P52737; -.
DR   BioGRID-ORCS; 7695; 10 hits in 1102 CRISPR screens.
DR   ChiTaRS; ZNF136; human.
DR   GenomeRNAi; 7695; -.
DR   Pharos; P52737; Tdark.
DR   PRO; PR:P52737; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P52737; protein.
DR   Bgee; ENSG00000196646; Expressed in secondary oocyte and 195 other tissues.
DR   ExpressionAtlas; P52737; baseline and differential.
DR   Genevisible; P52737; HS.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
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; 8.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 14.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 7.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..540
FT                   /note="Zinc finger protein 136"
FT                   /id="PRO_0000047420"
FT   DOMAIN          4..90
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         140..162
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         168..190
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         196..218
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         224..246
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         252..274
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         280..302
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         308..330
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         336..358
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         364..386
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         392..414
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         420..442
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         448..470
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         476..498
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         504..526
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         107
FT                   /note="Y -> C (in dbSNP:rs10425995)"
FT                   /id="VAR_033555"
SQ   SEQUENCE   540 AA;  62784 MW;  313297AB22F62952 CRC64;
     MDSVAFEDVD VNFTQEEWAL LDPSQKNLYR DVMWETMRNL ASIGKKWKDQ NIKDHYKHRG
     RNLRSHMLER LYQTKDGSQR GGIFSQFANQ NLSKKIPGVK LCESIVYGEV SMGQSSLNRH
     IKDHSGHEPK EYQEYGEKPD TRNQCWKPFS SHHSFRTHEI IHTGEKLYDC KECGKTFFSL
     KRIRRHIITH SGYTPYKCKV CGKAFDYPSR FRTHERSHTG EKPYECQECG KAFTCITSVR
     RHMIKHTGDG PYKCKVCGKP FHSLSSFQVH ERIHTGEKPF KCKQCGKAFS CSPTLRIHER
     THTGEKPYEC KQCGKAFSYL PSLRLHERIH TGEKPFVCKQ CGKAFRSAST FQIHERTHTG
     EKPYECKECG EAFSCIPSMR RHMIKHTGEG PYKCKVCGKP FHSLSPFRIH ERTHTGEKPY
     VCKHCGKAFV SSTSIRIHER THTGEKPYEC KQCGKAFSYL NSFRTHEMIH TGEKPFECKR
     CGKAFRSSSS FRLHERTHTG QKPYHCKECG KAYSCRASFQ RHMLTHAEDG PPYKCMWESL