ZN865_HUMAN
ID ZN865_HUMAN Reviewed; 1059 AA.
AC P0CJ78;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Zinc finger protein 865;
GN Name=ZNF865;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-802 AND LYS-1040, AND
RP 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: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AC008735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS58681.1; -.
DR RefSeq; NP_001182534.1; NM_001195605.1.
DR AlphaFoldDB; P0CJ78; -.
DR SMR; P0CJ78; -.
DR BioGRID; 936163; 45.
DR IntAct; P0CJ78; 13.
DR STRING; 9606.ENSP00000483134; -.
DR iPTMnet; P0CJ78; -.
DR PhosphoSitePlus; P0CJ78; -.
DR BioMuta; ZNF865; -.
DR DMDM; 322967615; -.
DR EPD; P0CJ78; -.
DR jPOST; P0CJ78; -.
DR MassIVE; P0CJ78; -.
DR MaxQB; P0CJ78; -.
DR PaxDb; P0CJ78; -.
DR PeptideAtlas; P0CJ78; -.
DR PRIDE; P0CJ78; -.
DR ProteomicsDB; 52492; -.
DR Antibodypedia; 69405; 41 antibodies from 12 providers.
DR DNASU; 100507290; -.
DR Ensembl; ENST00000568956.2; ENSP00000457715.1; ENSG00000261221.4.
DR GeneID; 100507290; -.
DR KEGG; hsa:100507290; -.
DR MANE-Select; ENST00000568956.2; ENSP00000457715.1; NM_001195605.2; NP_001182534.1.
DR UCSC; uc061dbu.1; human.
DR CTD; 100507290; -.
DR GeneCards; ZNF865; -.
DR HGNC; HGNC:38705; ZNF865.
DR HPA; ENSG00000261221; Tissue enhanced (skeletal).
DR neXtProt; NX_P0CJ78; -.
DR OpenTargets; ENSG00000261221; -.
DR VEuPathDB; HostDB:ENSG00000261221; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00530000064557; -.
DR HOGENOM; CLU_010472_0_0_1; -.
DR InParanoid; P0CJ78; -.
DR OMA; PTPQWGI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P0CJ78; -.
DR TreeFam; TF350857; -.
DR PathwayCommons; P0CJ78; -.
DR SignaLink; P0CJ78; -.
DR BioGRID-ORCS; 100507290; 11 hits in 1098 CRISPR screens.
DR GenomeRNAi; 100507290; -.
DR Pharos; P0CJ78; Tdark.
DR PRO; PR:P0CJ78; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P0CJ78; protein.
DR Bgee; ENSG00000261221; Expressed in gastrocnemius and 108 other tissues.
DR ExpressionAtlas; P0CJ78; baseline and differential.
DR Genevisible; P0CJ78; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; 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; 9.
DR SMART; SM00355; ZnF_C2H2; 20.
DR SUPFAM; SSF57667; SSF57667; 11.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 20.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 20.
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..1059
FT /note="Zinc finger protein 865"
FT /id="PRO_0000404594"
FT ZN_FING 224..246
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 252..274
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 350..372
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 378..400
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 407..429
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 441..463
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 550..572
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..600
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..628
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 669..691
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 697..719
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 792..814
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 820..842
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 848..870
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 876..898
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 904..926
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 932..954
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 960..982
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 989..1011
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1017..1039
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..141
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..296
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..498
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 802
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1040
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 1059 AA; 111077 MW; E7D8ECC3EDC1FBB4 CRC64;
MEANPAGSGA GGGGSSGIGG EDGVHFQSYP FDFLEFLNHQ RFEPMELYGE HAKAVAALPC
APGPPPQPPP QPPPPQYDYP PQSTFKPKAE VPSSSSSSSS SSSSSSSSSS SSSSSSSQAK
KPDPPLPPAF GAPPPPLFDA AFPTPQWGIV DLSGHQHLFG NLKRGGPASG PGVTPGLGAP
AGAPGPLPAP SQTPPGPPAA AACDPTKDDK GYFRRLKYLM ERRFPCGVCQ KSFKQSSHLV
QHMLVHSGER PYECGVCGRT YNHVSSLIRH RRCHKDVPPA AGGPPQPGPH LPPLGLPAPA
ASAATAAAPS TVSSGPPATP VAPAPSADGS AAPAGVGVPP PATGGGDGPF ACPLCWKVFK
KPSHLHQHQI IHTGEKPFSC SVCSKSFNRR ESLKRHVKTH SADLLRLPCG ICGKAFRDAS
YLLKHQAAHA GAGAGGPRPV YPCDLCGKSY SAPQSLLRHK AAHAPPAAAA EAPKDGAASA
PQPPPTFPPG PYLLPPDPPT TDSEKAAAAA AAVVYGAVPV PLLGAHPLLL GGAGTSGAGG
SGASVPGKTF CCGICGRGFG RRETLKRHER IHTGEKPHQC PVCGKRFRES FHLSKHHVVH
TRERPYKCEL CGKVFGYPQS LTRHRQVHRL QLPCALAGAA GLPSTQGTPG ACGPGASGTS
AGPTDGLSYA CSDCGEHFPD LFHVMSHKEV HMAEKPYGCD ACGKTFGFIE NLMWHKLVHQ
AAPERLLPPA PGGLQPPDGS SGTDAASVLD NGLAGEVGAA VAALAGVSGG EDAGGAAVAG
AGGGASSGPE RFSCATCGQS FKHFLGLVTH KYVHLVRRTL GCGLCGQSFA GAYDLLLHRR
SHRQKRGFRC PVCGKRFWEA ALLMRHQRCH TEQRPYRCGV CGRGFLRSWY LRQHRVVHTG
ERAFKCGVCA KRFAQSSSLA EHRRLHAVAR PQRCSACGKT FRYRSNLLEH QRLHLGERAY
RCEHCGKGFF YLSSVLRHQR AHEPPRPELR CPACLKAFKD PGYFRKHLAA HQGGRPFRCS
SCGEGFANTY GLKKHRLAHK AENLGGPGAG AGTLAGKDA
