ZN319_HUMAN
ID ZN319_HUMAN Reviewed; 582 AA.
AC Q9P2F9; Q52LH8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Zinc finger protein 319;
GN Name=ZNF319; Synonyms=KIAA1388;
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].
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130, 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 Q9P2F9; Q9BUH8: BEGAIN; NbExp=5; IntAct=EBI-11993110, EBI-742722;
CC Q9P2F9; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11993110, EBI-3867333;
CC Q9P2F9; Q92997: DVL3; NbExp=3; IntAct=EBI-11993110, EBI-739789;
CC Q9P2F9; O75791: GRAP2; NbExp=3; IntAct=EBI-11993110, EBI-740418;
CC Q9P2F9; O76011: KRT34; NbExp=3; IntAct=EBI-11993110, EBI-1047093;
CC Q9P2F9; Q6A162: KRT40; NbExp=3; IntAct=EBI-11993110, EBI-10171697;
CC Q9P2F9; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-11993110, EBI-12012928;
CC Q9P2F9; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-11993110, EBI-10171774;
CC Q9P2F9; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-11993110, EBI-10172052;
CC Q9P2F9; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-11993110, EBI-10241252;
CC Q9P2F9; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-11993110, EBI-22310682;
CC Q9P2F9; O75928-2: PIAS2; NbExp=3; IntAct=EBI-11993110, EBI-348567;
CC Q9P2F9; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-11993110, EBI-949255;
CC Q9P2F9; P78424: POU6F2; NbExp=3; IntAct=EBI-11993110, EBI-12029004;
CC Q9P2F9; P78317: RNF4; NbExp=5; IntAct=EBI-11993110, EBI-2340927;
CC Q9P2F9; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-11993110, EBI-725997;
CC Q9P2F9; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-11993110, EBI-11957238;
CC Q9P2F9; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-11993110, EBI-10252492;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92626.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB037809; BAA92626.1; ALT_INIT; mRNA.
DR EMBL; BC093919; AAH93919.1; -; mRNA.
DR EMBL; BC101767; AAI01768.1; -; mRNA.
DR CCDS; CCDS32462.1; -.
DR RefSeq; NP_065858.1; NM_020807.2.
DR RefSeq; XP_005256126.1; XM_005256069.3.
DR AlphaFoldDB; Q9P2F9; -.
DR SMR; Q9P2F9; -.
DR BioGRID; 121620; 25.
DR IntAct; Q9P2F9; 20.
DR STRING; 9606.ENSP00000299237; -.
DR iPTMnet; Q9P2F9; -.
DR PhosphoSitePlus; Q9P2F9; -.
DR BioMuta; ZNF319; -.
DR DMDM; 25091755; -.
DR EPD; Q9P2F9; -.
DR jPOST; Q9P2F9; -.
DR MassIVE; Q9P2F9; -.
DR MaxQB; Q9P2F9; -.
DR PaxDb; Q9P2F9; -.
DR PeptideAtlas; Q9P2F9; -.
DR PRIDE; Q9P2F9; -.
DR ProteomicsDB; 83809; -.
DR Antibodypedia; 29030; 99 antibodies from 19 providers.
DR DNASU; 57567; -.
DR Ensembl; ENST00000299237.3; ENSP00000299237.2; ENSG00000166188.3.
DR GeneID; 57567; -.
DR KEGG; hsa:57567; -.
DR MANE-Select; ENST00000299237.3; ENSP00000299237.2; NM_020807.3; NP_065858.1.
DR UCSC; uc002emx.2; human.
DR CTD; 57567; -.
DR DisGeNET; 57567; -.
DR GeneCards; ZNF319; -.
DR HGNC; HGNC:13644; ZNF319.
DR HPA; ENSG00000166188; Low tissue specificity.
DR neXtProt; NX_Q9P2F9; -.
DR OpenTargets; ENSG00000166188; -.
DR PharmGKB; PA134937483; -.
DR VEuPathDB; HostDB:ENSG00000166188; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160309; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; Q9P2F9; -.
DR OMA; QHHSAHT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9P2F9; -.
DR TreeFam; TF332615; -.
DR PathwayCommons; Q9P2F9; -.
DR SignaLink; Q9P2F9; -.
DR BioGRID-ORCS; 57567; 16 hits in 1103 CRISPR screens.
DR ChiTaRS; ZNF319; human.
DR GenomeRNAi; 57567; -.
DR Pharos; Q9P2F9; Tdark.
DR PRO; PR:Q9P2F9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9P2F9; protein.
DR Bgee; ENSG00000166188; Expressed in granulocyte and 125 other tissues.
DR ExpressionAtlas; Q9P2F9; baseline and differential.
DR Genevisible; Q9P2F9; 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; 7.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..582
FT /note="Zinc finger protein 319"
FT /id="PRO_0000047527"
FT ZN_FING 76..100
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 104..126
FT /note="C2H2-type 2; degenerate"
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 202..224
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 230..252
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 258..280
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 287..309
FT /note="C2H2-type 7; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 315..337
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 343..365
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 371..393
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 399..421
FT /note="C2H2-type 11; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 428..450
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 458..480
FT /note="C2H2-type 13; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 486..508
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 514..536
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 542..564
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
SQ SEQUENCE 582 AA; 65547 MW; E2FBD02256BE0A67 CRC64;
MSESWQQPPQ TQPQQPQPPQ PQHHAEPPPA LAEHTLPPGT AENPLGCAVY GILLQPDPGL
QPPQHAPLQA AGEPGPKCGV CGHDLAHLSS PHEHQCLAGH DRSFQCTQCL KIFHQATDLL
EHQCVQAEQK PFVCGVCKMG FSLLTSLAQH HSSHSGLVKC SICEKTYKPA EAAEPATTAA
PSLPAAPAPS TVTPAEQADK PYSCPICQKP FKHLSELSRH ERIHTGEKPY KCTLCDKSFS
QSSHLVHHKR THSSERPYKC AVCEKTFKHR SHLVRHMYAH SGEHHLFRCN VCELHFKESS
ELLQHPCTPS GERPFRCGEC QKAFKRPSDL RQHERTHSAE RPFKCDLCPM GFKQQYALMR
HRRTHKTEEP FKCGLCEKGF GQPSHLLYHQ HVHTLETLFK CPVCQKGFDQ SAELLRHKCL
PGAAERPFKC PVCNKAYKRA SALQKHQLAH CAAAEKPLRC TLCERRFFSS SEFVQHRCDP
AREKPLKCPD CEKRFKYASD LQRHRRVHTG EKPYKCPNCD KAFKQREHLN KHQGVHAREQ
QFKCVWCGER FLDVALLQEH SAQHSAAAAA AEGAYQVAAC LP
