ZN107_HUMAN
ID ZN107_HUMAN Reviewed; 783 AA.
AC Q9UII5;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Zinc finger protein 107;
DE AltName: Full=Zinc finger protein 588;
DE AltName: Full=Zinc finger protein ZFD25;
GN Name=ZNF107; Synonyms=ZFD25, ZNF588;
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=Brain;
RX PubMed=10673043; DOI=10.1016/s0167-4781(99)00206-7;
RA Li X.-A., Kokame K., Okubo K., Shimokado K., Tsukamoto Y., Miyata T.,
RA Kato H., Yutani C.;
RT "Cloning and characterization of a novel gene encoding a zinc finger
RT protein with 25 fingers.";
RL Biochim. Biophys. Acta 1489:405-412(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [3]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-186, AND IDENTIFICATION BY MASS
RP 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: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q9UII5; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-7234993, EBI-10961706;
CC Q9UII5; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-7234993, EBI-10171774;
CC Q9UII5; P26368-2: U2AF2; NbExp=3; IntAct=EBI-7234993, EBI-11097439;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, skeletal muscle, kidney
CC and pancreas. Weakly expressed in aorta, liver and lung.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AB027251; BAA85623.1; -; mRNA.
DR EMBL; BC047243; AAH47243.1; -; mRNA.
DR CCDS; CCDS5527.1; -.
DR RefSeq; NP_001013768.1; NM_001013746.2.
DR RefSeq; NP_057304.1; NM_016220.4.
DR RefSeq; XP_016867772.1; XM_017012283.1.
DR RefSeq; XP_016867773.1; XM_017012284.1.
DR RefSeq; XP_016867774.1; XM_017012285.1.
DR RefSeq; XP_016867775.1; XM_017012286.1.
DR AlphaFoldDB; Q9UII5; -.
DR SMR; Q9UII5; -.
DR BioGRID; 119533; 28.
DR IntAct; Q9UII5; 9.
DR MINT; Q9UII5; -.
DR STRING; 9606.ENSP00000483720; -.
DR iPTMnet; Q9UII5; -.
DR PhosphoSitePlus; Q9UII5; -.
DR BioMuta; ZNF107; -.
DR DMDM; 21542325; -.
DR EPD; Q9UII5; -.
DR jPOST; Q9UII5; -.
DR MassIVE; Q9UII5; -.
DR MaxQB; Q9UII5; -.
DR PaxDb; Q9UII5; -.
DR PeptideAtlas; Q9UII5; -.
DR PRIDE; Q9UII5; -.
DR ProteomicsDB; 84528; -.
DR Antibodypedia; 55871; 3 antibodies from 3 providers.
DR DNASU; 51427; -.
DR Ensembl; ENST00000344930.7; ENSP00000343443.3; ENSG00000196247.13.
DR Ensembl; ENST00000423627.6; ENSP00000400037.1; ENSG00000196247.13.
DR GeneID; 51427; -.
DR KEGG; hsa:51427; -.
DR UCSC; uc003tte.5; human.
DR CTD; 51427; -.
DR DisGeNET; 51427; -.
DR GeneCards; ZNF107; -.
DR HGNC; HGNC:12887; ZNF107.
DR HPA; ENSG00000196247; Tissue enhanced (lymphoid).
DR MIM; 603989; gene.
DR neXtProt; NX_Q9UII5; -.
DR OpenTargets; ENSG00000196247; -.
DR PharmGKB; PA37476; -.
DR VEuPathDB; HostDB:ENSG00000196247; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164280; -.
DR InParanoid; Q9UII5; -.
DR OMA; SVDECTE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9UII5; -.
DR TreeFam; TF343410; -.
DR PathwayCommons; Q9UII5; -.
DR SignaLink; Q9UII5; -.
DR BioGRID-ORCS; 51427; 12 hits in 1024 CRISPR screens.
DR ChiTaRS; ZNF107; human.
DR GenomeRNAi; 51427; -.
DR Pharos; Q9UII5; Tdark.
DR PRO; PR:Q9UII5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UII5; protein.
DR Bgee; ENSG00000196247; Expressed in secondary oocyte and 175 other tissues.
DR ExpressionAtlas; Q9UII5; baseline and differential.
DR Genevisible; Q9UII5; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 16.
DR SMART; SM00355; ZnF_C2H2; 22.
DR SUPFAM; SSF57667; SSF57667; 13.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 24.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..783
FT /note="Zinc finger protein 107"
FT /id="PRO_0000047681"
FT ZN_FING 76..98
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 104..126
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 132..154
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 160..182
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 188..210
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 216..238
FT /note="C2H2-type 6; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..266
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 272..294
FT /note="C2H2-type 8; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 9; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 12; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..490
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 524..546
FT /note="C2H2-type 17; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 552..574
FT /note="C2H2-type 18; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 580..602
FT /note="C2H2-type 19; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 608..630
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 636..658
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 664..686
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 692..714
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 720..742
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 748..770
FT /note="C2H2-type 25; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 783 AA; 90673 MW; 84882575525DC34C CRC64;
MVAKPPVMSF HFAQDLWPEQ NIKDSFQKVT LRRYGKCEYE NLQLRKGCKH VDECTGHKGG
HNTVNQCLTA TPSKIFQCNK YVKVFDKFSN SNRYKRRHTG NKHFKCKECS KSFCVLSQLT
QHRRIHTRVN SYKCEECGKA FNWFSTLTKH KRIHTGEKPY KCEECGKAFN QSSQLTRHKI
IHTEEKPNKC EECGKAFKQA SHLTIHKIIH TGEKPYKYEE CGKVFSQSSH LTTQKILHTG
ENLYKCKECG KAFNLFSNLT NHKRIHAGEK PYKCKECGRA FNISSNLNKQ EKIHTGGKLN
KCEECDKAFN RSLKLTAHKK ILMEEKPYKC EECGKVFNQF STLTRHKIIH TGEKPYKCKE
CGKAFNQSSN LTEHKKIHTA EKSYKCEECG KAFNQHSNLI NHRKIYSGEK PYKCEECGKA
FNRSSTLTRH KKIHTGEKPY KCEECDRAFS QSSNLTEHKK IHTGEKPYKC EECGKAFNRF
STLTKHKRIH TGEKPYKCEE CGKAFNQSYQ LTRHKIVHTK EKLNKCEEFG KAFKQSSHRT
IHKIIHTGEK PYKCEEHGKV FNQSSNLTTQ KIIHTGENLY KFEEHGKAFN LFSNITNHKI
IYTGEKPHKC EECGKAYNRF SNLTIHKRIH TGEKPYQCAE CGKAFNCSST LNRHKIIHTG
EKPYKCKECG KAFNLSSTLT AHKKIHTGEK PYKCEECGKA FNQSSNLTTH KKIHTSEKPY
KCEECGKSFN QFSSLNIHKI IHTGEKPYKC GDYGRAFNLS SNLTTHKKIH TGEKPYKCEY
GKT
